CMAH_GORGO
ID CMAH_GORGO Reviewed; 600 AA.
AC Q8MJC8; Q8MJC9; Q8WNM3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
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;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12192086; DOI=10.1073/pnas.182257399;
RA Chou H.-H., Hayakawa T., Diaz S., Krings M., Indriati E., Leakey M.,
RA Paabo S., Satta Y., Takahata N., Varki A.;
RT "Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to
RT brain expansion during human evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11736-11741(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-348.
RX PubMed=11948213; DOI=10.1093/jhered/92.6.469;
RA Stauffer R.L., Walker A., Ryder O.A., Lyons-Weiler M., Hedges S.B.;
RT "Human and ape molecular clocks and constraints on paleontological
RT hypotheses.";
RL J. Hered. 92:469-474(2001).
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; AF494222; AAN05317.1; -; mRNA.
DR EMBL; AF494223; AAN05318.1; -; mRNA.
DR EMBL; AF354635; AAL56239.1; -; mRNA.
DR AlphaFoldDB; Q8MJC8; -.
DR STRING; 9593.ENSGGOP00000004473; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR InParanoid; Q8MJC8; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000001519; 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..600
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000127800"
FT DOMAIN 9..107
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 70
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 CONFLICT 118
FT /note="D -> V (in Ref. 1; AAN05317)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="E -> K (in Ref. 2; AAL56239)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..348
FT /note="QPR -> HPP (in Ref. 2; AAL56239)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 600 AA; 69750 MW; 11749CD660A80DA3 CRC64;
QTTEILLCLS PVEVASLKEG INFFRNKSTG KDYILYKNKS RLRACKNMCK HQGGLFIKDI
EDLAGRSVRC TKHNWKLDVS TMKYINPPES FCQDELVVEM DENNRLLLLE LNPPNPWDLQ
PRSPEELAFG EVQITYLTHA CMDLKLGDKR MVFDPWLIGP AFARGWWLLH EPPSDWLERL
CQADLIYISH LHSDHLSYPT LKKLAGRRPD IPIYVGNTER PVFWNLNQSG VQLTNINVMP
FGIWQQVDKN LRFMILMDGV HPEMDTCIIV EYKGHKILNT VDCTRPNGGR LPMKVALMMS
DFAGGASGFP MTFSGGKFTE EWKAQFIKTE RKKLLNYKAR LVKNLQPRIY CPFAGYFVES
HPSDKYIKET NTKNDPNELN NLIKKNSDVI TWTPRPGATL DLGRMLKDPT DSKGIIEPPE
GTKIYKDSWD FEPYLEILNA AVGDEIFLHS SWIKEYFTWA GFKDYNLVVR MIETDEDFNP
FPGGYDYLVD FLDLSFPKER PQREHPYEEI HSRVDVIRHV VKNGLLWDEL YIGFQTRLQR
DPDIYHHLFW NHFQIKLPLT PPNWKSFLMC CEQNGPGILQ FSTERTNEPN RNKFSVENKA
