GenomeNet

Database: UniProt
Entry: H2FX23_OCESG
LinkDB: H2FX23_OCESG
Original site: H2FX23_OCESG 
ID   H2FX23_OCESG            Unreviewed;       457 AA.
AC   H2FX23;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:AEY02155.1};
GN   OrderedLocusNames=GU3_12000 {ECO:0000313|EMBL:AEY02155.1};
OS   Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Oceanimonas.
OX   NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY02155.1, ECO:0000313|Proteomes:UP000007742};
RN   [1] {ECO:0000313|EMBL:AEY02155.1, ECO:0000313|Proteomes:UP000007742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GK1 {ECO:0000313|EMBL:AEY02155.1,
RC   ECO:0000313|Proteomes:UP000007742};
RX   PubMed=22461556; DOI=10.1128/JB.00023-12;
RA   Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA   Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT   "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT   from Gavkhouni Wetland in Iran.";
RL   J. Bacteriol. 194:2123-2124(2012).
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|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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; CP003171; AEY02155.1; -; Genomic_DNA.
DR   RefSeq; WP_014292868.1; NC_016745.1.
DR   AlphaFoldDB; H2FX23; -.
DR   STRING; 511062.GU3_12000; -.
DR   KEGG; oce:GU3_12000; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_1_6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000007742; Chromosome.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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:AEY02155.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007742};
KW   Transferase {ECO:0000313|EMBL:AEY02155.1}.
SQ   SEQUENCE   457 AA;  49924 MW;  DBBC140402B38347 CRC64;
     MPELNKGALQ RLDEAHHLHP FTDSQSLHQK GARVIERGEG VYLWDADGHR ILDGMAGLWC
     VNLGYGREEL IEAANAQLRR LPYYNLFFQT THPPAARLAA TLAGLLPGDM QHLFFTGSGS
     ECNDTVVRMV RHFWAEQGRP ERKVIISRHN AYHGSTLAGA SLGGMKPMHA QGGLPLPDMV
     HIDQPYHFGE GQGTDPHAFG LARARQLEQK ILELGPERVA AFIGEPIQGA GGVIIPPDSY
     WPEIQRICRQ YDILLVADEV ICGFGRTGHW FASEHFGLEP DLLCMAKGIT SGYIPLGAVA
     VGRRVAEGLI AGGEFFHGFT YSGHPVACAV AQANIEVMQQ EHIVERVRDD IGPYLQQRWA
     SLADHPLVGE TRGLGLLAAL ELVADKATLA RFPSDAGAGL VCREHSLDAG LVMRAVGDTM
     IISPPLVITR AEIDELVEKA RRALDLTLHT LSNQQGK
//
DBGET integrated database retrieval system