The domain within your query sequence starts at position 564 and ends at position 838; the E-value for the HMGL-like domain shown below is 8.2e-29.

LLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNKLFSMENWGGATFDVAMRFLYEC
PWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNY
LPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKD
MAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMS
GMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEY

HMGL-like

HMGL-like
PFAM accession number:PF00682
Interpro abstract (IPR000891):

Pyruvate carboxylase (EC 6.4.1.1) (PC), a member of the biotin-dependent enzyme family, is involved in the gluconeogenesis by mediating the carboxylation of pyruvate to oxaloacetate. Biotin-dependent carboxylase enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as pyruvate [(PUBMED:11851389)]. PC has three functional domains: a biotin carboxylase (BC) domain, a carboxyltransferase (CT) domain which perform the second part of the reaction and a biotinyl domain [(PUBMED:7780827), (PUBMED:10229653)]. The mechanism by which the carboxyl group is transferred from the carboxybiotin to the pyruvate is not well understood.

The pyruvate carboxyltransferase domain is also found in other pyruvate binding enzymes and acetyl-CoA dependent enzymes suggesting that this domain can be associated with different enzymatic activities.

This domain is found towards the N-terminal region of various aldolase enzymes. This N-terminal TIM barrel domain [(PUBMED:12764229)] interacts with the C-terminal domain. The C-terminal DmpG_comm domain (IPR012425) is thought to promote heterodimerisation with members of IPR003361 to form a bifunctional aldolase-dehydrogenase [(PUBMED:12764229)].

GO function:catalytic activity (GO:0003824)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HMGL-like