ID A0A0B0H2A8_SOVGS Unreviewed; 394 AA.
AC A0A0B0H2A8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=JV46_24790 {ECO:0000313|EMBL:KHF24333.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF24333.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF24333.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF24333.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
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:KHF24333.1}.
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DR EMBL; JRAA01000003; KHF24333.1; -; Genomic_DNA.
DR RefSeq; WP_043118438.1; NZ_MPRZ01000002.1.
DR AlphaFoldDB; A0A0B0H2A8; -.
DR STRING; 2340.JV46_24790; -.
DR PATRIC; fig|2340.3.peg.2405; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000030856; 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:KHF24333.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KHF24333.1}.
FT DOMAIN 32..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 42955 MW; 00C06799F8746078 CRC64;
MSLKLSQRVQ AVKPSPTLAI TARAAELRAA GKDIIGLGAG EPDFDTPEHI QQAGIDAIKS
GKTRYTAVDG TASLKQAIID KFKRDNNFSF EADQILVSCG GKQSFYNLAQ AILDPGDEVI
IPAPYWVSYP DMAILAGGVP VYINADAEQN FKITPQQLET SITEATRLFV INSPSNPSGM
AYSMEELEAL GKVLESHPKI VIATDDMYEH ILWEGTSFCN ILNACPQLED RIIVLNGVSK
AYAMTGWRIG YAGGPVEIIK AMKKIQSQST SNPTSISQYA AETALNGPQS CINDMMVQFK
QRHDYVLDRF NRMPGIECLP SDGTFYLFPK ATDLIESLEG ISDDLQLADY LIQKAEVAVV
PGSAFGLAGY FRVSIATSME ELETAMDRIE KAIS
//
