CMAH_PONPY
ID CMAH_PONPY Reviewed; 585 AA.
AC Q8MJC6; Q8MJC7; Q8WNM4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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 11-507.
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}.
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; AF494224; AAN05319.1; -; mRNA.
DR EMBL; AF494225; AAN05320.1; -; mRNA.
DR EMBL; AF354634; AAL56238.1; -; mRNA.
DR AlphaFoldDB; Q8MJC6; -.
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..585
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000127806"
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 39
FT /note="K -> N (in Ref. 2; AAL56238)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..507
FT /note="REHPY -> ARTSL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="M -> T (in Ref. 1; AAN05319)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> K (in Ref. 1; AAN05319)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 585 AA; 68018 MW; 3358E9D397225AA6 CRC64;
QTTEILLCLS PVEVANLKEG INFFRNKSTG KDYILYKNKS RLRACKNMCK HQGGLFIKDI
EDLAGRSVRC TKHNWKLDVS TMKYINPPES FCQDELVVEM DENNRLLLLE LNPPNPWDLQ
PRSPEELAFG EVQITYLTHA CMDLKLGDKR MVFDPWLIGP AFARGWWLLH EPPSDWLERL
CQADLIYISH LHSDHLSYPT LKKLAGRRPD IPIYVGNTER PVFWNLNQSG VQLTNINIVP
FGIWQQVDKN LRFMILMDGV HPEMDTCIIV EYKGHKILNT VDCTRPNGGR LPMKVALMMS
DFAGGASGFP MTFSGGKFTE EWKAQFIKTE RKKLLNYKAQ LVKNLQPRIY CPFAGYFVES
HPSDKYIKET NTKNDPNELN NLIKKNSDVI TWTPRPGATL DLARMLKDPT DSKGIVEPPE
GTKIYKDSWD FEPYLEILNA AVGDEIFLHS SWIKEYFTWA GFKDYNLVVR MIETDEDFNP
FPGGYDYLVD FLDLSFPKER PQREHPYEEI HSRVDVIRHV VKNGLLWDEL YIGFQTRLQR
DPDIYHHLFW NHFQIKLPLM PPNWKSFLMC CEQNEPGILQ ECTTT
