Y737_HAEIN
ID Y737_HAEIN Reviewed; 265 AA.
AC O05031;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative uncharacterized protein HI_0737;
GN OrderedLocusNames=HI_0737;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Truncated acetolactase synthase; no longer catalytically
CC active.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; L42023; AAC22396.1; -; Genomic_DNA.
DR PIR; F64089; F64089.
DR RefSeq; NP_438896.1; NC_000907.1.
DR RefSeq; WP_005693141.1; NC_000907.1.
DR AlphaFoldDB; O05031; -.
DR SMR; O05031; -.
DR STRING; 71421.HI_0737; -.
DR EnsemblBacteria; AAC22396; AAC22396; HI_0737.
DR KEGG; hin:HI_0737; -.
DR PATRIC; fig|71421.8.peg.773; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_091591_0_0_6; -.
DR OMA; FTYVENQ; -.
DR PhylomeDB; O05031; -.
DR BioCyc; HINF71421:G1GJ1-775-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR PANTHER; PTHR18968; PTHR18968; 3.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
PE 5: Uncertain;
KW Lyase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..265
FT /note="Putative uncharacterized protein HI_0737"
FT /id="PRO_0000090814"
FT REGION 204..247
FT /note="Thiamine pyrophosphate binding"
FT BINDING 47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
SQ SEQUENCE 265 AA; 28784 MW; 79171AC8A5823144 CRC64;
MTGAQLIMAC LKAHHVTTLF GYPGGAIMPT YDALYDAGLD HLLCRNEQGT AMAAIGYARS
TGKVGVCIAT SGPGATNLVI GLGDAMMDSI PVVTITGQVA SPLIGTDAFQ EADVLGLSLA
CTKHSFIVQS ADVALQGDLI QALNALKQDL DIEPWREQIR NFKAKLDFTY VENQGNRPID
PWALLNSLSN RKPNNAIICT DVGQHQMWLV QHILRVARHC GFTVTTMEMT LIETQVRLKI
TVKSDRTLDL LVNQLVKLPD VLMVN
