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Database: UniProt
Entry: G9YC94_HAFAL
LinkDB: G9YC94_HAFAL
Original site: G9YC94_HAFAL 
ID   G9YC94_HAFAL            Unreviewed;       440 AA.
AC   G9YC94;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:EHM38707.1};
GN   ORFNames=HMPREF0454_04227 {ECO:0000313|EMBL:EHM38707.1};
OS   Hafnia alvei ATCC 51873.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM38707.1, ECO:0000313|Proteomes:UP000005959};
RN   [1] {ECO:0000313|EMBL:EHM38707.1, ECO:0000313|Proteomes:UP000005959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM38707.1,
RC   ECO:0000313|Proteomes:UP000005959};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM38707.1}.
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DR   EMBL; AGCI01000100; EHM38707.1; -; Genomic_DNA.
DR   RefSeq; WP_004096067.1; NZ_JH417552.1.
DR   AlphaFoldDB; G9YC94; -.
DR   PATRIC; fig|1002364.3.peg.3795; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   Proteomes; UP000005959; Unassembled WGS sequence.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; 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; ORNITHINE AMINOTRANSFERASE; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  46793 MW;  89EADB045E1A253C CRC64;
     MSENHNLSGN GTNQSWQKRR EEAVAGGVST LLPAFIQKAR NAELWDIEGN RYIDFAAGIA
     VLNTGHNHPK VIAAVQEQLT RFTHPCFQVT PYPEYVELAE RLNALVPIKE ATQTLLLTTG
     AEAVENAVKV ARIATGRGGV IAFRGGFHGR TLMGMALTGK VAPYKQGYGP FPSGIYHAPY
     PAPYLGITEQ HALDALDAIF AADIAPTEVA AIIIEPVQGE GGFYAAPAGF LKSLREICDR
     HGIVLIADEI QSGFCRTGKT FAIEHTGVEP DLVTMAKSLA GGFPLSALVG KKRLMEKALP
     GGLGGTYAGS PVAIAAALAV TDLIKDEQLN QKAQQVGEQI TRELHALAER FDCIGDIRAV
     GAMVAMELVE NRDATKPNKA LTSALVKEAG QQGLILLSCG VRGNVIRFLA PLTAEKEVIK
     EGMEKLAAAL SVVAKKVQNA
//
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