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   03-AUG-2022, entry version 91.
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-N-acetylneuraminate monooxygenase;
DE   AltName: Full=CMP-Neu5Ac hydroxylase;
DE   AltName: Full=CMP-NeuAc hydroxylase;
GN   Name=cmah;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; 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: Sialic acids are components of carbohydrate chains of
CC       glycoconjugates and are involved in cell-cell recognition and cell-
CC       pathogen interactions. Catalyzes the conversion of CMP-N-
CC       acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative
CC       CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly
CC       expressed at the surface of many cells. {ECO:0000250|UniProtKB:Q61419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + 2 Fe(II)-[cytochrome b5] + 2
CC         H(+) + O2 = CMP-N-glycoloyl-beta-neuraminate + 2 Fe(III)-[cytochrome
CC         b5] + H2O; Xref=Rhea:RHEA:16145, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:58376; EC=1.14.18.2;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; BC042338; AAH42338.1; -; mRNA.
DR   RefSeq; NP_001080297.1; NM_001086828.1.
DR   AlphaFoldDB; Q8AVF5; -.
DR   DNASU; 379989; -.
DR   GeneID; 379989; -.
DR   KEGG; xla:379989; -.
DR   CTD; 379989; -.
DR   Xenbase; XB-GENE-988338; cmah.L.
DR   OrthoDB; 569298at2759; -.
DR   UniPathway; UPA00628; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 379989; Expressed in zone of skin and 8 other tissues.
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:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03473; Rieske_CMP_Neu5Ac_hydrolase_N; 1.
DR   Gene3D; 2.102.10.10; -; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR037339; CMP-Neu5Ac_hydroxylase_Rieske.
DR   InterPro; IPR027033; Cnh.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   PANTHER; PTHR46522; PTHR46522; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Cytoplasm; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..591
FT                   /note="Cytidine monophosphate-N-acetylneuraminic acid
FT                   hydroxylase"
FT                   /id="PRO_0000127809"
FT   DOMAIN          16..114
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         58
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         77
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         80
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
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