ID   V4J5H5_9GAMM            Unreviewed;       395 AA.
AC   V4J5H5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=N838_19880 {ECO:0000313|EMBL:ESQ09684.1};
OS   Thiohalocapsa sp. PB-PSB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiohalocapsa.
OX   NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ09684.1, ECO:0000313|Proteomes:UP000017935};
RN   [1] {ECO:0000313|EMBL:ESQ09684.1, ECO:0000313|Proteomes:UP000017935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA   Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA   Orphan V.J.;
RT   "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT   consortia of the Sippewissett salt marsh.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC       ECO:0000256|RuleBase:RU000481}.
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:ESQ09684.1}.
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DR   EMBL; AVFR01001236; ESQ09684.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4J5H5; -.
DR   PATRIC; fig|1385625.5.peg.7378; -.
DR   Proteomes; UP000017935; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ESQ09684.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017935};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ESQ09684.1}.
FT   DOMAIN          33..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   395 AA;  42374 MW;  378354C57EB93D55 CRC64;
     MTIKLSARVQ SVKPSATLAI TARAKELRAA GQDVIGLGAG EPDFDTPEHI KQAAIAAIHD
     GFTKYTAVDG TPELKRAVMD KFRRDNGLDY TPDQILVSCG GKQSFFNMAQ AVLEPGDEVV
     IPAPYWVSYP DMVLLAGAAP VLVHAGAEQR FKITASQLKA AMNEQTRMVV INSPSNPTGM
     AYSSDELAAL GEVLREFPKA LIATDDMYEH IRWDTASPFV NILNVCPDLG PRTLVLNGVS
     KAYSMTGWRI GYAGGPEQVI KAMKKVQSQS TSNPTSISQV AAQAALEGPQ DCIGEMLKAF
     KERHDFVVDA LNRISGIECL PTDGTFYVFP KVQGLIDRLA GVGNDLELAE HLIEKAGVAL
     VPGSAFGLGG YARISIATSR QNLEQALQRI ADTAV
//