ID L1NCZ2_9BACT Unreviewed; 459 AA.
AC L1NCZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Putative 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000313|EMBL:EKY01233.1};
GN ORFNames=HMPREF9151_01091 {ECO:0000313|EMBL:EKY01233.1};
OS Hoylesella saccharolytica F0055.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKY01233.1, ECO:0000313|Proteomes:UP000010433};
RN [1] {ECO:0000313|EMBL:EKY01233.1, ECO:0000313|Proteomes:UP000010433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0055 {ECO:0000313|EMBL:EKY01233.1,
RC ECO:0000313|Proteomes:UP000010433};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|RuleBase:RU000363}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKY01233.1}.
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DR EMBL; AMEP01000074; EKY01233.1; -; Genomic_DNA.
DR RefSeq; WP_009162305.1; NZ_KB290987.1.
DR AlphaFoldDB; L1NCZ2; -.
DR STRING; 1127699.HMPREF9151_01091; -.
DR PATRIC; fig|1127699.3.peg.1004; -.
DR HOGENOM; CLU_049603_0_0_10; -.
DR Proteomes; UP000010433; Unassembled WGS sequence.
DR GO; GO:0070567; F:cytidylyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR012115; CDP-ribitol_syn.
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 PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01128; IspD; 1.
DR PIRSF; PIRSF036586; CDP-ribitol_syn; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000313|EMBL:EKY01233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010433};
KW Transferase {ECO:0000313|EMBL:EKY01233.1}.
SQ SEQUENCE 459 AA; 51112 MW; F6D3E0E74F97820E CRC64;
MIKKHNIAVI LAGGIGQRAG ISMPKQFFKV AGKMVIEHTI DVFERNKGID EIAIVSNPLL
ISDIENIVLK NGWKKVKRIL KGGNERYESS LSAIQAYDNE AVNLIFHDAV RPLLSQRILN
DVLEALKKHT AIDVAMPSAD TIIEVAGDFI HTIPDRSRLR RGQTPQAFAI EVIREAYEKA
LGDPAFKTTD DCGVVKKYLP QVPIYVVMGE ESNMKLTYKE DTYMLDKLFQ LKNTEAEHVD
LSTLDLNGKV AIVFGGSYGI GADTVQLLTE RGAKVYNFSR SNNGIDVGKR EDVAAAIRQV
VDAEKHIDYV VNTAGLLNKE PLTAMDYETI LYSVQTNYLG VVNVALESYP FLRKSKGRLV
FFTSSSYTRG RAFYSIYSST KAAIVNFVQA VAQEWEADGI CINCINPERT KTPMRVKNFG
IEPDDTLLPS QQVAEATLRT LVSDYTGQVI DVRRAHDEH
//
