ID Q2SBF7_HAHCH Unreviewed; 374 AA.
AC Q2SBF7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase {ECO:0000313|EMBL:ABC32017.1};
GN OrderedLocusNames=HCH_05345 {ECO:0000313|EMBL:ABC32017.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC32017.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC32017.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC32017.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP000155; ABC32017.1; -; Genomic_DNA.
DR RefSeq; WP_011399081.1; NC_007645.1.
DR AlphaFoldDB; Q2SBF7; -.
DR STRING; 349521.HCH_05345; -.
DR KEGG; hch:HCH_05345; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_6; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABC32017.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:ABC32017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Transferase {ECO:0000313|EMBL:ABC32017.1}.
FT DOMAIN 14..336
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 374 AA; 40697 MW; 4ADE8E9429FA35E6 CRC64;
MSTGFTIPNR LLLGPGPSNT PASVLAAMSQ PTIGHLDPVF INMMDQIKQM LQVTFKTHNR
LTMPVSAPGS AGMETCLVNL LEPGDQAIVA VNGVFGKRMV ENVVRAGGVP IVVEFEWGRP
VDPQRIKEVL NEHPQARLLA FVHAETSTGA RSDAETLCCL AHERGVLSVV DMVTSWCGIE
VDVDGWKADA VYSGAQKCLS AVPGIAPVTF SEKAADRIRT RTKPVQSWFL DMSLVMAYWA
EGGQRAYHHT APVNTLYAIH EALRLVLDEG LENRWARHKA AHEALVKGME SLGLSFLVEE
PYRLPMLNAI KVPEGVNEAV VRNKLLTDYN MEIGAGLGPL QGKIWRIGLM GNNATVECAN
RAVSALDECL QALK
//
