ID   D0KX60_HALNC            Unreviewed;       440 AA.
AC   D0KX60;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ACX97180.1};
GN   OrderedLocusNames=Hneap_2371 {ECO:0000313|EMBL:ACX97180.1};
OS   Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS   neapolitanus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX97180.1, ECO:0000313|Proteomes:UP000009102};
RN   [1] {ECO:0000313|EMBL:ACX97180.1, ECO:0000313|Proteomes:UP000009102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Kerfeld C., Cannon G., Heinhort S.;
RT   "Complete sequence of Halothiobacillus neapolitanus c2.";
RL   Submitted (OCT-2009) 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   ---------------------------------------------------------------------------
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; CP001801; ACX97180.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0KX60; -.
DR   STRING; 555778.Hneap_2371; -.
DR   KEGG; hna:Hneap_2371; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9770449at2; -.
DR   Proteomes; UP000009102; Chromosome.
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; 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   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:ACX97180.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009102};
KW   Transferase {ECO:0000313|EMBL:ACX97180.1}.
SQ   SEQUENCE   440 AA;  47057 MW;  6810A67453CF4384 CRC64;
     MTAHAMTKSA QTTAPNDQSM NADLQARRLA ATPRGVGVMA GFYIDRAQNA EVWDVEGNRY
     IDFAGGIAVL NTGHRHPALV AAIEEQLKRF THTCYQVLPY ESYVRLAERI NALVPGHYAK
     KTAFFSSGAE AVENAVKIAR SSTGRPGIIA FSGGFHGRTM MGCALTGKVV PYKVGFGPFP
     SEVYHLPFPM ELHGVTVEDS LHALETLFKA EIEPSRVAAI IIEPVQGEGG FYVAPPQLLH
     GLRKVCDEHG ILLIFDEVQT GFGRTGKLFA TEYYDVLPDI VTMAKSMAGG MTLSAVCGRA
     EVMDAPAPGG LGGTYAGNPL AIAAALAVID VMEKEQLVER SNFLGEKLMA RLNAAQAAVP
     ALKEVRGLGS MVAAEFCDPA TGAPSPDAVK RVQQAALEEG LILLTCGVYA NVIRFLYPLT
     TEDTVFDEAL DILDRALAKA
//