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Database: UniProt
Entry: G4FB44_9GAMM
LinkDB: G4FB44_9GAMM
Original site: G4FB44_9GAMM 
ID   G4FB44_9GAMM            Unreviewed;       394 AA.
AC   G4FB44;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:EHA14335.1};
GN   ORFNames=HAL1_18141 {ECO:0000313|EMBL:EHA14335.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14335.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA14335.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:EHA14335.1}.
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DR   EMBL; AGIB01000084; EHA14335.1; -; Genomic_DNA.
DR   RefSeq; WP_008959485.1; NZ_CP130610.1.
DR   AlphaFoldDB; G4FB44; -.
DR   PATRIC; fig|550984.5.peg.3510; -.
DR   Proteomes; UP000005692; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EHA14335.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:EHA14335.1}.
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         188
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   394 AA;  43752 MW;  2FDA7014E289BE48 CRC64;
     MLNGPFSPWP SFTEEEAQAI QRVLLSNQVN YWTGQEGRQF EREFAAYSGT EYAIAVSNGT
     TAIDLALKGL STGEGHCHDE VIVTSRTFLA SVSSIATAGA IPVFADVGRD SQNITAATIA
     EKITPNTRAI IVVHLAGWPC EMDSIMTLAE QHGLYVIEDC AQAHGATYKG RSVGSIGHVG
     CWSFCQDKIM TTGGEGGMVT TKDETLWRKM WAYKDHGKSW EAVYEREHPP GFRWLHESFG
     TNWRLTEMQA AIGRIQLARM PEWKAARQAN AQHIWQTAND CAGLRVPKVP EHIEHAAYKC
     YVFVEPEKLN EAWSRDRIMA EIIKQGVPCF SGSCSEVYLE KAFDGTGYRP DEPLPVAREL
     GETSLMFLCH PTLTEAEINK TCLILKQVMA KATQ
//
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