CMAH_PANTR
ID CMAH_PANTR Reviewed; 590 AA.
AC O97598;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9751737; DOI=10.1073/pnas.95.20.11751;
RA Chou H.-H., Takematsu H., Diaz S., Iber J., Nickerson E., Wright K.L.,
RA Muchmore E.A., Nelson D.L., Warren S.T., Varki A.;
RT "A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-
RT Pan divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11751-11756(1998).
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; AF074481; AAC68882.1; -; mRNA.
DR RefSeq; NP_001009041.1; NM_001009041.1.
DR AlphaFoldDB; O97598; -.
DR STRING; 9598.ENSPTRP00000030365; -.
DR PaxDb; O97598; -.
DR GeneID; 450121; -.
DR KEGG; ptr:450121; -.
DR CTD; 12763; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR HOGENOM; CLU_034056_0_0_1; -.
DR InParanoid; O97598; -.
DR TreeFam; TF331273; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000002277; 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_0000127804"
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; 68448 MW; 68313BBACFDEC696 CRC64;
MGSIEQTTEI LLCLSPVEVA SLKEGINFFR NKSTGKDYIL YKNKSRLRAC KNMCKHQGGL
FIKDIEDLAG RSVRCTKHNW KLDVSTMKYI NPPESFCQDE LVVEMDENNR LLLLELNPPN
PWDLQPRSPE ELAFGEVQIT YLTHACMDLK LGDKRMVFDP WLIGPAFARG WWLLHEPPSD
WLERLCQADL IYISHLHSDH LSYPTLKKLA GRRPDIPIYV GNTERPVFWN LNQSGVQLTN
INVVPFGIWQ QVDKNLRFMI LMDGVHPEMD TCIIVEYKGH KILNTVDCTR PNGGRLPMKV
ALMMSDFAGG ASGFPMTFSG GKFTEEWKAQ FIKTERKKLL NYKARLVKNL QPRIYCPFAG
YFVESHPSDK YIKETNTKND PNELNNLIKK NSDVITWTPR PGATLDLGRM LKDPTDSKGI
IEPPEGTKIY KDSWDFEPYL EILNAAVGDE IFLHSSWIKE YFTWAGFKDY NLVVRMIETD
EDFNPFPGGY DYLVDFLDLS FPKERPQREH PYEEIHSRVD VIRHVVKNGL LWDELYIGFQ
TRLQRDPDIY HHLFWNHFQI KLPLTPPNWK SFLMCCEQNG PGILQECKTT
