ID   CMAH_DANRE              Reviewed;         591 AA.
AC   Q6GML1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 131.
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; ORFNames=zgc:92407;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2004) 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] + O2
CC         + 2 H(+) = 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC074033; AAH74033.1; -; mRNA.
DR   RefSeq; NP_001002192.1; NM_001002192.1.
DR   AlphaFoldDB; Q6GML1; -.
DR   FunCoup; Q6GML1; 121.
DR   STRING; 7955.ENSDARP00000141882; -.
DR   PaxDb; 7955-ENSDARP00000141882; -.
DR   PeptideAtlas; Q6GML1; -.
DR   Ensembl; ENSDART00000080439; ENSDARP00000074888; ENSDARG00000057714.
DR   Ensembl; ENSDART00000166058; ENSDARP00000141882; ENSDARG00000057714.
DR   GeneID; 431739; -.
DR   KEGG; dre:431739; -.
DR   AGR; ZFIN:ZDB-GENE-040704-33; -.
DR   CTD; 12763; -.
DR   ZFIN; ZDB-GENE-040704-33; cmah.
DR   eggNOG; ENOG502QR0M; Eukaryota.
DR   GeneTree; ENSGT00390000010830; -.
DR   InParanoid; Q6GML1; -.
DR   OMA; WKSFLMC; -.
DR   OrthoDB; 332863at2759; -.
DR   PhylomeDB; Q6GML1; -.
DR   UniPathway; UPA00628; -.
DR   PRO; PR:Q6GML1; -.
DR   Proteomes; UP000000437; Chromosome 4.
DR   Bgee; ENSDARG00000057714; Expressed in intestine and 18 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0046381; P:CMP-N-acetylneuraminate metabolic process; IBA:GO_Central.
DR   GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03473; Rieske_CMP_Neu5Ac_hydrolase_N; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 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; CYTIDINE MONOPHOSPHATE-N-ACETYLNEURAMINIC ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR46522:SF1; INACTIVE CYTIDINE MONOPHOSPHATE-N-ACETYLNEURAMINIC ACID HYDROXYLASE; 1.
DR   Pfam; PF13483; Lactamase_B_3; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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_0000127808"
FT   DOMAIN          12..110
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         52
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         54
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         73
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         76
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   591 AA;  68297 MW;  9462314CEF46A49E CRC64;
     MAAQVSHTVL RLEAEDVRNL KDGINFQKNN KDGKCYIIYK ANGELRACRN QCKHQGGLFI
     KDIEDMDGRT VRCTKHYWKL NVATMQYVNP PDSFMQDELE AVLSETDGSL ELLELNPPDP
     WTAEPREAQD LQAGEITLTY ITHACMELKA GERRMMFDPW LTGPAFARGW WLLHEPPKDA
     MDRLMEADLV YISHMHSDHL SYPTLQHLSK KRPDIPIYVG NTSRPVFWYL EKSGVNLTNI
     NVVPFGVWQN VDDHLRFMIL MDGVHPEMDT CLIVEYKGHM ILNTVDCTRP NNGRLPHGVD
     VMMSDFAGGA SGFPMTFHGG KYTESWKANF IKNERKKLLN YKAQLVKSLQ PKIYCPFAGY
     FTEAHPSDRY IKETNTKNSP AELNELIRKS CLNTLTWTPL PGSVLDLAVA LNNRSNETAI
     TDPPHGTKIY KDNWEFDLYL NQLNASISAE IFKHKHWIQY YYNWAGFRNY NLVIRVIETD
     DDFQPLNGGF DYLVDFLDLS FPTERPEREH AYEEIKNRVN VMRHVVVNGL LWDDLYIGFN
     NRMSRDPDVY HHKFWNHFQT ELPLSAPDWQ HFLQICSQTQ ENGSSNGCSV S
//