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Database: UniProt
Entry: A0A0Q9YRC9_9COXI
LinkDB: A0A0Q9YRC9_9COXI
Original site: A0A0Q9YRC9_9COXI 
ID   A0A0Q9YRC9_9COXI        Unreviewed;       365 AA.
AC   A0A0Q9YRC9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE            EC=4.2.1.47 {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE   AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
GN   Name=gmd_1 {ECO:0000313|EMBL:KRG22457.1};
GN   Synonyms=gmd {ECO:0000256|HAMAP-Rule:MF_00955};
GN   ORFNames=HT99x_00880 {ECO:0000313|EMBL:KRG22457.1};
OS   Candidatus Berkiella aquae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Berkiella.
OX   NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG22457.1, ECO:0000313|Proteomes:UP000051497};
RN   [1] {ECO:0000313|EMBL:KRG22457.1, ECO:0000313|Proteomes:UP000051497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HT99 {ECO:0000313|EMBL:KRG22457.1,
RC   ECO:0000313|Proteomes:UP000051497};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC       deoxy-D-mannose. {ECO:0000256|HAMAP-Rule:MF_00955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC         Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57964; EC=4.2.1.47; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00955};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00001937,
CC         ECO:0000256|HAMAP-Rule:MF_00955};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009263, ECO:0000256|HAMAP-Rule:MF_00955}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00955}.
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:KRG22457.1}.
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DR   EMBL; LKAJ01000002; KRG22457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9YRC9; -.
DR   STRING; 295108.HT99x_00880; -.
DR   PATRIC; fig|1590043.3.peg.884; -.
DR   Proteomes; UP000051497; Unassembled WGS sequence.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR   CDD; cd05260; GDP_MD_SDR_e; 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   HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR   InterPro; IPR006368; GDP_Man_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01472; gmd; 1.
DR   PANTHER; PTHR43715:SF1; GDP-MANNOSE 4,6 DEHYDRATASE; 1.
DR   PANTHER; PTHR43715; GDP-MANNOSE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00955, ECO:0000313|EMBL:KRG22457.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051497}.
FT   DOMAIN          9..339
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   365 AA;  41559 MW;  547351E0057E4818 CRC64;
     MTESIKRALI TGITGQDGSY LAEFLLEKGY EVHGIKRRTS LFNTDRIDHL YQDPHVAKRR
     LVLHHGDLTD SSSLIRIIQQ VQPDEIYNLA AQSHVAVSFE EPEYTANADA IGTLRLLEAI
     RILGLEKKTR FYQASTSELF GKVQTIPQNE ATPFYPRSPY AVAKLYAHWI TINYREAYNI
     FACNGILFNH ESPVRGETFV TRKITRALAR IKLGLQDCLY LGNLDSLRDW GHAKDYVEMQ
     WLMLQQDNPD DYVIASGEQH SVREFVTIAA KELGITMRWE GQGEQEKGFD AASGACLVAV
     DPRYYRPTEV DTLLGDATKA KHKLGWTPKI SFEALVKEMV VEDFKLAQKD ALCQKEGFKV
     FEYQE
//
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