CMAH_MACMU
ID CMAH_MACMU Reviewed; 590 AA.
AC Q9TUJ2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Irie A., Suzuki A.;
RT "Molecular evolution of CMP-NeuAc hydoxylase in primates.";
RL Submitted (MAY-1998) 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; AB013814; BAA86057.1; -; mRNA.
DR RefSeq; NP_001028028.2; NM_001032856.2.
DR AlphaFoldDB; Q9TUJ2; -.
DR STRING; 9544.ENSMMUP00000007844; -.
DR GeneID; 574186; -.
DR KEGG; mcc:574186; -.
DR CTD; 12763; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR InParanoid; Q9TUJ2; -.
DR OrthoDB; 569298at2759; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000006718; Unplaced.
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..590
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000127802"
FT DOMAIN 14..112
FT /note="Rieske"
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 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 590 AA; 68256 MW; 334B8474A2908A95 CRC64;
MGSTEQTTEI LLCLSPVEVA NLKEGINFFR NKSTGKDYIL YKSKSRLRAC KNVCKHQGGL
FIKDIEDLAG RSVRCTKHNW KLDVSTMKYI NPPESFCQDE LVVEMDENNG LLLLELNPPN
PWDSEPRSPE ELDFGEVQIT YLTHACMDLK LGDKRMVFDP WLIGPAFARG WWLLHEPPSD
WLERLCQADL IYISHLHSDH LSYPTLKKLA GRRPDIPIYV GNTERPVFWN LNQSGVQLTN
INVVPFGIWQ QVDKNLRFMI LMDGVHPEMD TCIIVEYKGH KILNTVDCTR PNGGRLPTKV
ALMMSDFAGG ASGFPMTFSG GKFTEEWKAQ FIKTERKKLL NYKAQLVKNL QPRIYCPFAG
YFVESHPSDK YIKETNTKND PNELNNLIKK NSDVITWTPR PGATLDLGRM LKDPTDSKGI
IEPPEGTKIY KDSWDFEPYL EILNAAVGDE IFLHSSWIKE YFTWAGFKDY NLVVRMIETD
EDFNPFPGGY DYLVDFLDLS FPKERPQREH PYEEIRSRVD VIRHVVKNGL LWDELYIGFQ
TRLQRDPDIY HHLFWNHFQI KLPLTPPNWR SFLTCCEQNG PGISQECKTT
