Y1556_HAEIN
ID Y1556_HAEIN Reviewed; 315 AA.
AC P45250;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative 2-hydroxyacid dehydrogenase HI_1556;
DE EC=1.-.-.-;
GN OrderedLocusNames=HI_1556;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L42023; AAC23205.1; -; Genomic_DNA.
DR PIR; F64129; F64129.
DR RefSeq; NP_439705.1; NC_000907.1.
DR RefSeq; WP_005693583.1; NC_000907.1.
DR AlphaFoldDB; P45250; -.
DR SMR; P45250; -.
DR STRING; 71421.HI_1556; -.
DR PRIDE; P45250; -.
DR EnsemblBacteria; AAC23205; AAC23205; HI_1556.
DR KEGG; hin:HI_1556; -.
DR PATRIC; fig|71421.8.peg.1627; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
DR OMA; PHIAWAY; -.
DR PhylomeDB; P45250; -.
DR BioCyc; HINF71421:G1GJ1-1576-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..315
FT /note="Putative 2-hydroxyacid dehydrogenase HI_1556"
FT /id="PRO_0000076034"
FT ACT_SITE 233
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 156..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 231..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 285..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 34636 MW; 0023D28C3266689B CRC64;
MKIVFLDSTA IPKHISIPRP SFEHTWTEYE HTSAEQTIER VKDADIVITS KVIFDRETLQ
QLPKLKLIAI TATGTNNVDL VAAEEMGIAV RNVTGYSSTT VPEHVIGLIF SLKHSLAGWL
RDQTEAKWAE SKQFCYFDYP ITDVRGSTLG VFGKGCLGTE VGRLANAVGM KVLYAEHKDA
TVCREGYTPF DEVLKQADIV TLHCPLTETT KDLINAETLS KMKKGAFLIN TGRGPLIDEL
ALVDALKTGH LGGAALDVMV KEPPEKDNPL ILAAKTMPNL IITPHIAWAS DSAVTTLVGK
VMQNIEEFVQ QLHQK