ACS1_HAEIF
ID ACS1_HAEIF Reviewed; 474 AA.
AC Q48154;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1 {ECO:0000303|PubMed:10094675};
DE Includes:
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000303|PubMed:10094675};
DE EC=2.7.7.40 {ECO:0000269|PubMed:10094675};
DE Includes:
DE RecName: Full=Ribulose-5-phosphate reductase {ECO:0000303|PubMed:10094675};
DE Short=Ribulose-5-P reductase {ECO:0000305};
DE EC=1.1.1.405 {ECO:0000269|PubMed:10094675};
DE AltName: Full=Ribitol-5-phosphate dehydrogenase {ECO:0000305};
GN Name=acs1 {ECO:0000303|PubMed:10094675};
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727 {ECO:0000312|EMBL:CAA85750.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9006 / AMC 36-A-3 / Serotype A {ECO:0000312|EMBL:CAA85750.1};
RX PubMed=10094675; DOI=10.1128/jb.181.7.2001-2007.1999;
RA Follens A., Veiga-da-Cunha M., Merckx R., an Schaftingen E., van Eldere J.;
RT "acs1 of Haemophilus influenzae type a capsulation locus region II encodes
RT a bifunctional ribulose 5-phosphate reductase- CDP-ribitol
RT pyrophosphorylase.";
RL J. Bacteriol. 181:2001-2007(1999).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of D-ribulose 5-
CC phosphate to D-ribitol 5-phosphate and the further reaction of D-
CC ribitol 5-phosphate with CTP to form CDP-ribitol.
CC {ECO:0000269|PubMed:10094675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol +
CC diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608,
CC ChEBI:CHEBI:57695; EC=2.7.7.40;
CC Evidence={ECO:0000269|PubMed:10094675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate +
CC H(+) + NADPH; Xref=Rhea:RHEA:19921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57695, ChEBI:CHEBI:57783, ChEBI:CHEBI:58121,
CC ChEBI:CHEBI:58349; EC=1.1.1.405;
CC Evidence={ECO:0000269|PubMed:10094675};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for D-ribulose 5-phosphate (in the presence of 50 uM CTP)
CC {ECO:0000269|PubMed:10094675};
CC KM=400 uM for D-ribulose 5-phosphate (in the absence of CTP)
CC {ECO:0000269|PubMed:10094675};
CC KM=10 uM for NADPH {ECO:0000269|PubMed:10094675};
CC KM=37 uM for D-ribitol 5-phosphate (for the cytidylyltransferase
CC reaction) {ECO:0000269|PubMed:10094675};
CC KM=150 uM for CTP {ECO:0000269|PubMed:10094675};
CC Vmax=9.55 umol/min/mg enzyme (for the reductase reaction in the
CC absence of CTP) {ECO:0000269|PubMed:10094675};
CC Vmax=27.9 umol/min/mg enzyme (for the reductase reaction in the
CC presence of 50 uM CTP) {ECO:0000269|PubMed:10094675};
CC Vmax=15.7 umol/min/mg enzyme (for the cytidylyltransferase reaction)
CC {ECO:0000269|PubMed:10094675};
CC pH dependence:
CC Optimum pH is 7-8.4 for D-ribulose 5-phosphate reductase activity.
CC {ECO:0000269|PubMed:10094675};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
CC cytidylyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the short-chain
CC dehydrogenases/reductases (SDR) family. {ECO:0000305}.
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DR EMBL; Z37516; CAA85750.1; -; Genomic_DNA.
DR AlphaFoldDB; Q48154; -.
DR SMR; Q48154; -.
DR BRENDA; 1.1.1.405; 2529.
DR UniPathway; UPA00934; -.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00108; IspD; 1.
DR InterPro; IPR012115; CDP-ribitol_syn.
DR InterPro; IPR001228; IspD.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF01128; IspD; 1.
DR PIRSF; PIRSF036586; CDP-ribitol_syn; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; NADP; Nucleotidyltransferase;
KW Oxidoreductase; Transferase.
FT CHAIN 1..474
FT /note="Bifunctional ribulose 5-phosphate reductase/CDP-
FT ribitol pyrophosphorylase Acs1"
FT /id="PRO_0000437505"
FT REGION 1..238
FT /note="Ribitol-5-phosphate cytidylyltransferase"
FT REGION 250..474
FT /note="Ribulose-5-phosphate reductase"
SQ SEQUENCE 474 AA; 52438 MW; A8FEBE0FF6452BF7 CRC64;
MLKNKNIGII LAGGIGSRMG LGYPKQFSKI AGKTALEHTI FIFQEHKEID EIIIVSERTS
YRRIEDIVSK AGFSKVNRII FGGKERSDST LSAITALQDE PRNTKLIIHD AVRPLLATEI
ISECIAKLDK YNAVDVAIPA VDTIVHVNND TQEIIKIPKR AEYYQGQTPQ AFKLGTLKKA
YDIYTQGGIE GTCDCSIVLK TLPEERVGIV SGFETNIKLT RPVDLFIADK LFQSRSHFSL
RNITSIDRLY DMKDQVLVVI GGSYGIGAHI IDVAKKFGIK TYSLSRSNGV DVGDVKSIEK
AFAGIYGKEH KIDHIVNTAA VLNHKTLASM SYEEIVTSIN VNYTGMINAV ITAYPYLKQT
HGSFLGFTSS SYTRGRPFYA IYSSAKAAVV NLTQAISEEW LPDNIKINCV NPERTKTPMR
TKAFGIEPEG TLLDPKTVAF ASLTVLASRE TGNIIDVVLK DEEYISHILA DLYK
