ID   M7MHP2_9FLAO            Unreviewed;       396 AA.
AC   M7MHP2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Acetylornithine aminotransferase (ACOAT) {ECO:0000313|EMBL:EMQ94616.1};
GN   ORFNames=D778_00570 {ECO:0000313|EMBL:EMQ94616.1};
OS   Xanthomarina gelatinilytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Xanthomarina.
OX   NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ94616.1, ECO:0000313|Proteomes:UP000012024};
RN   [1] {ECO:0000313|EMBL:EMQ94616.1, ECO:0000313|Proteomes:UP000012024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK20 {ECO:0000313|EMBL:EMQ94616.1,
RC   ECO:0000313|Proteomes:UP000012024};
RA   Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Formosa sp. AK20.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:EMQ94616.1}.
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DR   EMBL; ANLA01000015; EMQ94616.1; -; Genomic_DNA.
DR   RefSeq; WP_007650237.1; NZ_ANLA01000015.1.
DR   AlphaFoldDB; M7MHP2; -.
DR   PATRIC; fig|1137281.3.peg.2002; -.
DR   eggNOG; COG4992; Bacteria.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000012024; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   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; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EMQ94616.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012024};
KW   Transferase {ECO:0000313|EMBL:EMQ94616.1}.
SQ   SEQUENCE   396 AA;  43392 MW;  C0A324DEF5EF392F CRC64;
     MAEDFLKYQA QTSPHPLAMK VSHAKGSYIY DVNNKAYLDF VAGVSACTLG HGHPKVVAAI
     KEQLDQYLHV MVYGEYIQEP AVELAKFLAK NLPNNLEKTY LTNSGTEAIE GALKLAKRAT
     GRSGIVSAKN AYHGNTMGSM SVMGYEERKR AFRPLLPDVS FMEFNNEEDL SKITKKTAGV
     ILETIQGGAG FIEPKNHYLE KVRERCDKVG ALLILDEIQP GIGRTGKLFG FEHYNCVPDI
     LVTGKGLGGG MPIGAFTASG KLMDLLQDKP KLGHITTFGG HPVIAAAALA TLKEVTKSDL
     MAQTLEKEQL FRKHLAHPLI LDIRGKGLML AAITPSADIT NQVILACQDE GLILFWLLFE
     PKAIRITPPL TITKEEIIKG CQIILKVLDE IQEKHS
//