ID A0A2P2DY12_9LEPT Unreviewed; 407 AA.
AC A0A2P2DY12;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|ARBA:ARBA00019930};
DE EC=3.5.4.26 {ECO:0000256|ARBA:ARBA00012766};
GN ORFNames=LPTSP4_10310 {ECO:0000313|EMBL:GBF49517.1};
OS Leptospira ryugenii.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1917863 {ECO:0000313|EMBL:GBF49517.1, ECO:0000313|Proteomes:UP000245133};
RN [1] {ECO:0000313|EMBL:GBF49517.1, ECO:0000313|Proteomes:UP000245133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH101 {ECO:0000313|EMBL:GBF49517.1,
RC ECO:0000313|Proteomes:UP000245133};
RA Nakao R., Masuzawa T.;
RT "Novel Leptospira species isolated from soil and water in Japan.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-
CC phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-
CC phosphate. {ECO:0000256|ARBA:ARBA00002151}.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004882}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase
CC family. {ECO:0000256|ARBA:ARBA00007417}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259}.
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:GBF49517.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BFBB01000003; GBF49517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2DY12; -.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000245133; Unassembled WGS sequence.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01284; Riboflavin_deaminase-reductase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR002734; RibDG_C.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245133}.
FT DOMAIN 4..117
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 407 AA; 46480 MW; D38F178B3349235A CRC64;
MESSALKNIL LQIRKLSFLA MGMSSPNPPV ACVLANPNGE ILSQAHTQTT GKNHAEREAY
ENWSQNVGDH IAIVSLEPCT HFGRTPPCRD LILEARPKEL WIGWKDPNPL IESGNWDTYK
SLGIQAKLNP ILAKVSYPYL FGFIQRIQRK RPWIWIKSAL TTSFHYAPTD SRQVAISSEA
SRPYLQMLRA KFDAVLVGPN TVSVDEPSLN FRLEESVSAY PAKQMFYEIK DSFFSAGRGL
LDDLFQFCSE EILQEHSSNH KKYQPFRIFC ISENQTLSDS FLRKQKSLNE EYTSQKVIFI
FLGKDANLHP QYAQMAELTE FPIPNFSRRE GSVCLEWLAE LGINTLLCEA GSFVWEFFHE
NLMPGDCILT IQGKIEFESG KVFAGMEAGR EVSEYQVQED IWRLREI
//
