CMAH_CRIGR
ID CMAH_CRIGR Reviewed; 563 AA.
AC Q9WV23;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
DE Flags: Fragment;
GN Name=CMAH; Synonyms=CNAH;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=12880951; DOI=10.1016/s0304-4165(03)00137-5;
RA Chenu S., Gregoire A., Malykh Y., Visvikis A., Monaco L., Shaw L.,
RA Schauer R., Marc A., Goergen J.-L.;
RT "Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in
RT engineered Chinese hamster ovary cells using an antisense-RNA strategy.";
RL Biochim. Biophys. Acta 1622:133-144(2003).
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:0000269|PubMed:12880951}.
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 Evidence={ECO:0000269|PubMed:12880951};
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; AJ242835; CAB44648.1; -; mRNA.
DR AlphaFoldDB; Q9WV23; -.
DR STRING; 10029.XP_007634620.1; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR UniPathway; UPA00628; -.
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; Transport.
FT CHAIN <1..>563
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000127799"
FT DOMAIN 10..108
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT NON_TER 1
FT NON_TER 563
SQ SEQUENCE 563 AA; 65105 MW; F62726BA5429359D CRC64;
KQTAETLLSL SPAETANLKE GINFFRNKTT GKEYILYKEK NHLKACKNLC KHQGGLFIKD
IEDLDGRSVK CTKHNWKLDV STMKYINPPG SFCQDELVVE MDGNDGLFLI ELNPPNPWDS
DPRTPEELAF GEVQITYLTH ACMDLKLGDK RMVFDPWLIG PAFARGWWLL HEPPSDWLER
LCKADLIYIS HMHSDHLSYP TLKQLSQRRP DIPIYVGDTE RPVFWNLDQS GVQLTNINVV
PFGVWQQVDK NLRFMILMDG VHPEMDTCII VEYKGHKILN TVDCTRPNGG RLPEKAALMM
SDFAGGASGF PMTFSGGKFT EEWKAQFIKA ERRKLLNYKA QLVKDLQPRI YCPFAGYFVE
SHPSDKYIKE TNIKNDPIQL NNLIKKNCDV VTWTPRPGAT LDLGRMLKDP TDSQGIIEPP
EGTKIYKDSW DFGPYLSTLH SAVGDEIFLH SSWIKEYFTW AGFKSYNLVV RMIETDEDFN
PFPGGYDYLV DFLDLSFPKE RPSREHPYEE IRSRVDVVRY VVKHGLLWDD LYIGFQTRLQ
RDPDIYHHLF WNHFQIKLPL TPP
