HIS8_GLUDA
ID HIS8_GLUDA Reviewed; 356 AA.
AC A9H311; B5ZF55;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN OrderedLocusNames=GDI0282, Gdia_2345;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; AM889285; CAP54225.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI52099.1; -; Genomic_DNA.
DR RefSeq; WP_012222533.1; NC_010125.1.
DR AlphaFoldDB; A9H311; -.
DR SMR; A9H311; -.
DR STRING; 272568.GDI0282; -.
DR EnsemblBacteria; ACI52099; ACI52099; Gdia_2345.
DR EnsemblBacteria; CAP54225; CAP54225; GDI0282.
DR KEGG; gdi:GDI0282; -.
DR KEGG; gdj:Gdia_2345; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_0_5; -.
DR OMA; FDGYPIL; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000084195"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT CONFLICT 315
FT /note="A -> G (in Ref. 2; ACI52099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 39008 MW; 8B182EEC073DD851 CRC64;
MSRFWSPVVH RLTPYVPGEQ PKLTNLIKLN TNESPYGPPP GALEAIRAAA DDTLRLYSDP
TSERLRAAIA QAHDVGMDEI FVGNGSDEVL AHAFHALLQH DAPLLTPDIT YSFYPVYCGL
YGIAHQPVPL DDAMRIDVDD YRRPCAGLVL PNPNAPTGIA LGLGQIETLL RAQPDRVVVI
DEAYVDFGAD TAIPLVRRFP NLLVVRTLSK SHALAGLRVG YAIGHPDLVE ALNRVKDSFN
SYPLDRLAQA GAAAAIADRE WLARTTGKII KTRIGLTSSL RGLGFEVLPS QANFVFARHP
DRDAAHLAAA LRERAIIVRH FRTPRIAEWL RITVGTDEEC RVLTDALGTI LTRNAD
