ID   CMAH_XENLA              Reviewed;         591 AA.
AC   Q8AVF5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Cytidine monophosphate-N-acetylneuraminic acid hydroxylase;
DE            Short=CMP-N-acetylneuraminic acid hydroxylase;
DE            EC=1.14.18.2;
DE   AltName: Full=CMP-Neu5Ac hydroxylase;
DE   AltName: Full=CMP-NeuAc hydroxylase;
DE   AltName: Full=CMP-N-acetylneuraminate monooxygenase;
GN   Name=cmah;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of CMP-N-acetylneuraminic acid
CC       (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-
CC       glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly
CC       expressed at the surface of many cells (By similarity).
CC   -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + 2 ferrocytochrome b5
CC       + O(2) + 2 H(+) = CMP-N-glycoloylneuraminate + 2 ferricytochrome
CC       b5 + H(2)O.
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminic acid
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; BC042338; AAH42338.1; -; mRNA.
DR   RefSeq; NP_001080297.1; -.
DR   UniGene; Xl.76765; -.
DR   GeneID; 379989; -.
DR   KEGG; xla:379989; -.
DR   Xenbase; XB-FEAT-988334; cmah.
DR   HOVERGEN; Q8AVF5; -.
DR   BRENDA; 1.14.18.2; 648.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   Pfam; PF00355; Rieske; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Cytoplasm; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Transport.
FT   CHAIN         1    591       Cytidine monophosphate-N-acetylneuraminic
FT                                acid hydroxylase.
FT                                /FTId=PRO_0000127809.
FT   DOMAIN       16    114       Rieske.
FT   METAL        56     56       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        58     58       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL        77     77       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        80     80       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
SQ   SEQUENCE   591 AA;  68369 MW;  2051BEB6807E988C CRC64;
     MEQSNDGQTA HTLLHLASAE VESLKEGITF LRNKESGKNF IIYKNGEELR ACKNLCKHQG
     GTFIKDIEDL GNRTVRCTKH NWKLDVSSMK YVNPPDSFCQ DELVIENDDE NGVSLVELSP
     PNPWDSDPRM AVCLEGGEVQ VTYLTHACMD LKLGNKHMVF DPWLIGPAFA RGWWLLHEPP
     CDWLERLCRA DLIYISHMHS DHLSYPTLKK LSEKRPDIPI YVGKTERPVF WYLDKSGVKL
     TNINVVPFGI WQEVDENLRF MILMDGVHPE MDTCIIVEYK GNKILNTVDC TRPNGGKLPT
     NVALMMSDFA GGASGFPMTF SGGKFTEEWK SQFIKTERKK LLNYKAQLVK DLNPRIYCPF
     AGYFVEEHPS DKYIKETNLK NDAAELNMLI RNTSDVVTWT PKPGAILDLG RLLIDPTDKN
     GIIDPPPGTK IFKDSWDYDT YLSIHSFSFD DEIFHYPSWI KEYFTWAGFK GYNLVLRMIE
     TDEHFVPLPK GYNYLVDFLD LSFPTERPER DHPYEEISSR ATVIRHVVKH GLLWDDLYIG
     FQTRIQRNPD IYHHQFWNHF QIKLPLTPPD WKVFLDREKE NNATLQNCSI M
//