ID D0LXY3_HALO1 Unreviewed; 367 AA.
AC D0LXY3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Serine--pyruvate transaminase {ECO:0000313|EMBL:ACY14338.1};
DE EC=2.6.1.51 {ECO:0000313|EMBL:ACY14338.1};
GN OrderedLocusNames=Hoch_1789 {ECO:0000313|EMBL:ACY14338.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14338.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY14338.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP001804; ACY14338.1; -; Genomic_DNA.
DR RefSeq; WP_012826946.1; NC_013440.1.
DR AlphaFoldDB; D0LXY3; -.
DR STRING; 502025.Hoch_1789; -.
DR KEGG; hoh:Hoch_1789; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_7; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR CDD; cd06451; AGAT_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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACY14338.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:ACY14338.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Transferase {ECO:0000313|EMBL:ACY14338.1}.
FT DOMAIN 30..328
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 367 AA; 39416 MW; 411A43A840465121 CRC64;
MDTSTPERVL MGPGPSDVPA RVLQALARPT VGHLDPFFLR CMDEIRSRLR TVFATENEMT
LAVSGTGSAG METLFVNLVE PGDKVLVGRC GVFGNRMSDV AERCGGEVVT VDAPWGQPIE
PGQMIKAIEQ HKPKVVAIVH AETSTGVHQP LDGIADATHE VGGLLLLDCV TSLGGMPVEI
DAWGVDAAYS GTQKCLSCPP GLAPVTLSSR AVQRLDARKH KVQSWYLDLS MVRNYWGGER
AYHHTAPVNM LYALHEALGM VLEEGLEARF ARHREVHGTL RDGLDELGVS FVSAAGFRLP
MLNAVGVPAG VDDAGTRKRL LEDYGIEIGG GLGDFRGKAW RIGLMGHAAS LRNVTLLLAA
LRDITRG
//
