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Database: UniProt
Entry: A0A061SSG5_9RHOB
LinkDB: A0A061SSG5_9RHOB
Original site: A0A061SSG5_9RHOB 
ID   A0A061SSG5_9RHOB        Unreviewed;       431 AA.
AC   A0A061SSG5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KAJ04651.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:KAJ04651.1};
GN   ORFNames=PM02_00015 {ECO:0000313|EMBL:KAJ04651.1};
OS   Sulfitobacter mediterraneus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ04651.1, ECO:0000313|Proteomes:UP000027337};
RN   [1] {ECO:0000313|EMBL:KAJ04651.1, ECO:0000313|Proteomes:UP000027337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ04651.1,
RC   ECO:0000313|Proteomes:UP000027337};
RX   PubMed=24855294;
RA   Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT   "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT   Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT   Mallorca Island (Mediterranean Sea).";
RL   Genome Announc. 2:e00350-14(2014).
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   -!- 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:KAJ04651.1}.
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DR   EMBL; JEMU01000001; KAJ04651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061SSG5; -.
DR   STRING; 83219.PM02_00015; -.
DR   eggNOG; COG0160; Bacteria.
DR   Proteomes; UP000027337; Unassembled WGS sequence.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; 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; IPR004632; 4NH2But_aminotransferase_bac.
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   NCBIfam; TIGR00700; GABAtrnsam; 1.
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.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KAJ04651.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027337};
KW   Transferase {ECO:0000313|EMBL:KAJ04651.1}.
SQ   SEQUENCE   431 AA;  45376 MW;  F456B3C781961D50 CRC64;
     MTNAELVARR DASVARGVAS AAPIYASRAE NSELWDVEGN RYVDFAGGIA VLNTGHRHPK
     VIAAAKAQED HYTHTSFQVV PYEPYVALAE KLNALAPGDH AKKSLLVTTG AEAVENAVKI
     ARAATGRPGV IAFTGGYHGR TLLTLGMTGK VSPYKKDIGP FPSDIFRAPF PSLRDGITVE
     DALTGLQNLF LTDAQPERVA AIIIEPVLGE GGYTPVPFEM MQALREICDT HGILLIADEI
     QAGFGRTGTW FAVEHSGVVP DLITVAKSMA GGYPIAGVIG RAEVMDAVIP GGLGGTYGGN
     PVACAAALAA IEAIEEEGLL ARSTALGEHF RTRFSEIGAR VAPFRMWDIR GLGAMLAVEF
     VTDFETATPD ADLTKAVVAH ALKRGLILLA CGMHGNALRI MVPLTASDAI IDEGIAIFEE
     ALVAAIAEQN A
//
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