ID A0A086ZMJ6_9BIFI Unreviewed; 431 AA.
AC A0A086ZMJ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
DE Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
DE EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
GN Name=argD {ECO:0000256|HAMAP-Rule:MF_01107};
GN ORFNames=BBIA_2438 {ECO:0000313|EMBL:KFI47746.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI47746.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI47746.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI47746.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01107};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01107};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01107};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP-
CC Rule:MF_01107}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01107}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI47746.1}.
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DR EMBL; JGYN01000033; KFI47746.1; -; Genomic_DNA.
DR RefSeq; WP_033493196.1; NZ_JGYN01000033.1.
DR AlphaFoldDB; A0A086ZMJ6; -.
DR STRING; 1437608.GCA_000771645_02437; -.
DR eggNOG; COG4992; Bacteria.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000029108; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01107};
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW ECO:0000313|EMBL:KFI47746.1};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01107}; Reference proteome {ECO:0000313|Proteomes:UP000029108};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:KFI47746.1}.
FT BINDING 118..119
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 157
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 160
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 251..254
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 313
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 314
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ SEQUENCE 431 AA; 45459 MW; D6F47A47B50A6052 CRC64;
MVTEQTEKLG SEDSKWLGEY SQVHMNVFGT PLRVLDHGQG AHVWDVDGNE YLDFLAGIAV
NSIGYAHPKW VKAVSEQAAK VAHTSNYFAT EPQIKLAAKL VELAGAPEGS HVYFGNSGAE
GNEAAIKLAK LYGRTLPGAT PSIGGKPARI IALTHGFHGR TLGALSATWK PSIRTPFEPL
VPGIEFVEAG NPMALYEAFA QTGQGHYGKG PVAAVIMELI QGEAGVRPLG ADYVKKVRQM
CDINHALLII DEVQTGMGRT GKWFAFQRED LSGGVTPDMV TFAKGVAGGF PMGGMIAFGS
KLSALFTPGS HGSTFAGNPL GAAASLATIG VIEDENLVAN AEARGQQLRD GIMATGNPLF
ESARGRGLLD AVQLSHPCAH AVMNWALEHG LIVNAVAPDA LRFAPPLNVT AQDVDQALAI
LARIPDDLPN D
//
