ID   A0A162M3P9_9FIRM        Unreviewed;       428 AA.
AC   A0A162M3P9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:KYO63793.1};
DE            EC=2.6.1.11 {ECO:0000313|EMBL:KYO63793.1};
GN   Name=argD {ECO:0000313|EMBL:KYO63793.1};
GN   ORFNames=ATZ99_22730 {ECO:0000313|EMBL:KYO63793.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO63793.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO63793.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO63793.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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:KYO63793.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LOHZ01000047; KYO63793.1; -; Genomic_DNA.
DR   RefSeq; WP_068749365.1; NZ_LOHZ01000047.1.
DR   AlphaFoldDB; A0A162M3P9; -.
DR   STRING; 520767.ATZ99_22730; -.
DR   PATRIC; fig|520767.4.peg.2406; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000075737; Unassembled WGS sequence.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:RHEA.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KYO63793.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075737};
KW   Transferase {ECO:0000313|EMBL:KYO63793.1}.
SQ   SEQUENCE   428 AA;  47117 MW;  D3179CAD37DBE325 CRC64;
     MNTVEKYKEY VNTSMVKAIE PVVIERAKGA IIYSEDGKEY IDCFSGISVV NAGHCNEEVL
     KAAKEQMEKL VHACTYVYYI KPVADLAEKL AQITPGRLKK TFFANSGAEA NEAAMRAAKQ
     FTGRYEFIAL QCSFHGRSVG TLSITGNMAR KKGGGPYLSG TAFSPAPYCY RCSFGLSYPN
     CELRCAKFLE DIIRFHTSGN VAAFFAEPVM GEGGIIVPPP EYFKVVKEIL DRYGILFVAD
     EVQSGFGRTG KLFAIEYYDV EPDELTMAKG IADGFPLGAF IAREEVANSF KPGDHLSTFG
     GNPVSCAAAI ANIDFIIKND ICFQVVEKGK WFMEKLIELK QEFKIIGDVR GKGLMIGLEL
     VKDDKKTPAA EEADMLRNLC REKGILVGLG GVNGNVIRIQ PPLIISKDQL DYAFNVIKEN
     ISKIEKAN
//