ID A0A0J7BKU1_9BACT Unreviewed; 398 AA.
AC A0A0J7BKU1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE Short=OAT {ECO:0000256|HAMAP-Rule:MF_01689};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587, ECO:0000256|HAMAP-Rule:MF_01689};
GN Name=rocD {ECO:0000256|HAMAP-Rule:MF_01689,
GN ECO:0000313|EMBL:KMP11007.1};
GN ORFNames=UZ36_05890 {ECO:0000313|EMBL:KMP11007.1};
OS Candidatus Nitromaritima sp. SCGC AAA799-C22.
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Candidatus Nitromaritima.
OX NCBI_TaxID=1628279 {ECO:0000313|EMBL:KMP11007.1, ECO:0000313|Proteomes:UP000036407};
RN [1] {ECO:0000313|EMBL:KMP11007.1, ECO:0000313|Proteomes:UP000036407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC_AAA799_C22 {ECO:0000313|EMBL:KMP11007.1};
RA Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT "Diversification and niche adaptations of Nitrospina-like bacteria in the
RT poly-extreme interfaces of the Atlantis II Deep brine from the Red Sea.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01689};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004998, ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01689}.
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:KMP11007.1}.
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DR EMBL; JZKJ01000032; KMP11007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7BKU1; -.
DR PATRIC; fig|1628279.3.peg.933; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000036407; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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_01689; Ornith_aminotrans_3; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR034757; Ornith_aminotrans_bact.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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|HAMAP-Rule:MF_01689};
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689,
KW ECO:0000313|EMBL:KMP11007.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_01689};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01689}; Reference proteome {ECO:0000313|Proteomes:UP000036407};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01689, ECO:0000313|EMBL:KMP11007.1}.
FT MOD_RES 254
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01689"
SQ SEQUENCE 398 AA; 44060 MW; A644854B79B67FFE CRC64;
MDTQDFIRLE TEYGAHNYNP LDVVLTRGEG IWVWDVEGDK YLDCLSSYSA VNQGHCHPKI
LKAMNEQAKK LTLVSRAFRN DQLGPFYKEI CELTHSHSVL PMNSGAEAVE TSIKAIRKWG
YQVKKVPAGL AEIIVCDNNF HGRTLTIVGF STEEQYRDGY APFTPGFKSI PFGDTGALEK
TITPNTVGFL VEPIQGEGGV IVPPAGYLKS VREICDRHNV MLILDEIQTG LGRTGKLFAE
EHEGIESDLT LIGKALSGGF YPVSAVLSNK EVLGVFNPGD HGSTFGGNPL ACAVAREALK
VLVEENLVDN AATQGEYFMK QLRQIDSPHV KEVRGRGLLI GIELSPESGG ARRFCEALRE
EKILCKETHQ HVIRFAPPLT IQRENIDWAL ERIRKVLV
//
