CMAH_DANRE
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 03-AUG-2022, entry version 116.
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] + 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; BC074033; AAH74033.1; -; mRNA.
DR RefSeq; NP_001002192.1; NM_001002192.1.
DR AlphaFoldDB; Q6GML1; -.
DR STRING; 7955.ENSDARP00000074888; -.
DR PaxDb; Q6GML1; -.
DR Ensembl; ENSDART00000080439; ENSDARP00000074888; ENSDARG00000057714.
DR Ensembl; ENSDART00000166058; ENSDARP00000141882; ENSDARG00000057714.
DR GeneID; 431739; -.
DR KEGG; dre:431739; -.
DR CTD; 12763; -.
DR ZFIN; ZDB-GENE-040704-33; cmah.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR GeneTree; ENSGT00390000010830; -.
DR InParanoid; Q6GML1; -.
DR OMA; GERRFMF; -.
DR OrthoDB; 569298at2759; -.
DR PhylomeDB; Q6GML1; -.
DR TreeFam; TF331273; -.
DR UniPathway; UPA00628; -.
DR PRO; PR:Q6GML1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000057714; Expressed in intestine and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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_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
