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Database: UniProt
Entry: B8HBI9_PSECP
LinkDB: B8HBI9_PSECP
Original site: B8HBI9_PSECP 
ID   B8HBI9_PSECP            Unreviewed;       474 AA.
AC   B8HBI9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   OrderedLocusNames=Achl_2412 {ECO:0000313|EMBL:ACL40377.1};
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL40377.1, ECO:0000313|Proteomes:UP000002505};
RN   [1] {ECO:0000313|EMBL:ACL40377.1, ECO:0000313|Proteomes:UP000002505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC   NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC       yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC         rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62830; EC=1.1.1.133;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00010154}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
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DR   EMBL; CP001341; ACL40377.1; -; Genomic_DNA.
DR   RefSeq; WP_015937589.1; NC_011886.1.
DR   AlphaFoldDB; B8HBI9; -.
DR   STRING; 452863.Achl_2412; -.
DR   KEGG; ach:Achl_2412; -.
DR   eggNOG; COG1091; Bacteria.
DR   eggNOG; COG1898; Bacteria.
DR   HOGENOM; CLU_045518_6_2_11; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000002505; Chromosome.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
DR   GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00438; cupin_RmlC; 1.
DR   CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000888; RmlC-like.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR   PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT   DOMAIN          191..468
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   SITE            140
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-3"
SQ   SEQUENCE   474 AA;  51534 MW;  01AB98F5F519AB5C CRC64;
     MSLEFSKKLS GHTTPIPGVV LYDLPVHGDN RGWFKENWQR EKMVALGLPD FRPVQNNISF
     NEKAGTTRGI HAEPWDKFIS VATGRIFGAW VDLREGPSFG AVFTAELDPS QAIFIPRGVG
     NAFQTLEDNT AYTYLVNDHW SADAQGQYTF LNLADETAAV SWPIPLDQAE LSDKDKAHPR
     MADVTPMPAK KVLVVGADGQ LGKALREQYD GEARVEFAGR GEFDLAREDS FKNRNWKNYS
     AIVNAAAYTA VDAAESEEGR AAAWAINVTA VANLARTAVE HDLTLVHVSS DYVFDGSRDN
     HGENEPLTPL GVYGQTKAAG EAVAGVVPRH YIVRTSWVIG EGSNFVRTMA SLAGRGIKPA
     VVNDQTGRLS FTRDIAAFIS HLLTTEAAYG TYNFSNDGPV KSWADIAADV YEQVGASRTD
     VTGVTTAEYF KDKAAAPRPL KSALNLAKAH STGFDVANAD ERLTAYLKAE NDKA
//
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