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Database: UniProt
Entry: A0A011AJF2_9ACTN
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ID   A0A011AJF2_9ACTN        Unreviewed;       336 AA.
AC   A0A011AJF2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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 {ECO:0000256|HAMAP-Rule:MF_00955};
GN   ORFNames=CryarDRAFT_3288 {ECO:0000313|EMBL:EXG82146.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG82146.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG82146.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG82146.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) 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:EXG82146.1}.
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DR   EMBL; JFBT01000001; EXG82146.1; -; Genomic_DNA.
DR   RefSeq; WP_035851743.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A011AJF2; -.
DR   PATRIC; fig|927661.3.peg.3246; -.
DR   HOGENOM; CLU_007383_14_0_11; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000021053; 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};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053}.
FT   DOMAIN          5..315
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   336 AA;  37777 MW;  29CC78C56F3E8B2B CRC64;
     MTVALITGIT GQDGSYLAEL LLRKGYEVHG LKRRSSSFNT DRIDRFDSDL WDPDAGFFQH
     YADLADGASL AHLLCRIQPD EIYHLGAQSH VRVSFDLPGY TTDITGMGTV RLLEAIRVAG
     LDCRFYQASS SEMFGATPPP QSETAPFHPR SPYGCAKVLG YWATVNHREA WGLKATNGIL
     FNHESPRRGE TFVTRKITRA VARIEAGLQD VLYLGNLDAI RDWGYAPEYV EAMWMMVQHP
     EPDDFVIATG EAHSVREFVV AAFAQAGLDW ERYVRIDPSY YRPSEVDVLI GDASKAERVL
     GWTPKTRFSD LVRIMVDADR QLLDDERSGR LVRVDI
//
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