CMAH_ASTRU
ID CMAH_ASTRU Reviewed; 653 AA.
AC Q95V11;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, 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;
GN Name=cnh;
OS Asterias rubens (Common European starfish) (Asterias vulgaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Forcipulatacea; Forcipulatida; Asteriidae; Asterias.
OX NCBI_TaxID=7604;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ENZYME ACTIVITY.
RC TISSUE=Gonad;
RX PubMed=11589708; DOI=10.1046/j.0014-2956.2001.02446.x;
RA Martensen I., Schauer R., Shaw L.;
RT "Cloning and expression of a membrane-bound CMP-N-acetylneuraminic acid
RT hydroxylase from the starfish Asterias rubens.";
RL Eur. J. Biochem. 268:5157-5166(2001).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12524037; DOI=10.1016/s1096-4959(02)00190-2;
RA Gollub M., Shaw L.;
RT "Isolation and characterization of cytidine-5'-monophosphate-N-
RT acetylneuraminate hydroxylase from the starfish Asterias rubens.";
RL Comp. Biochem. Physiol. 134B:89-101(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:11589708}.
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:11589708};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.94 uM for cytochrome b5 {ECO:0000269|PubMed:12524037};
CC KM=9.76 uM for CMP-Neu5Ac {ECO:0000269|PubMed:12524037};
CC Vmax=58.7 pmol/min/mg enzyme with cytochrome b5 as substrate
CC {ECO:0000269|PubMed:12524037};
CC Vmax=9.76 pmol/min/mg enzyme with CMP-Neu5Ac as substrate
CC {ECO:0000269|PubMed:12524037};
CC Note=Decreased enzyme activity in presence of 100 mM of NaCl.;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; AJ308602; CAC67678.1; -; mRNA.
DR AlphaFoldDB; Q95V11; -.
DR SMR; Q95V11; -.
DR PRIDE; Q95V11; -.
DR SABIO-RK; Q95V11; -.
DR UniPathway; UPA00628; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..653
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000127807"
FT TRANSMEM 630..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..120
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 596..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 653 AA; 75336 MW; 521FCFD239418897 CRC64;
MEQEREIVFS LSPEETSELK NGVNLISRSE KEKFVIYKDP TAENTVEEPA TSHMYKACLN
KCKHQGGTFI KDIEDGDNCI LRCTKHGWKL DAKTMRYVNP PDSFSQQQLV PEYNEDGSLD
IVELKPPQPW ETDKRDPMPL EVGEVQITYF THACIEIKLG DLIMFTDPWL IGPAFARGWW
LMHEPPADWL DRLAKADLIY ISHLHSDHLN YPTLELLSQR NPDIPIYVGD TSMPVFVRLE
QSGVKLNNIH IKKFGKWIEI NKDTRFMIMM DGVHPDMDTC ALIDYKGHLI LDTVDCTNPN
GGRLPIGVDM MLSDFAGGAS GFPMTFSGGK YTEEWKAEFV KRERRKLLYY KMQQVRDVAP
TVYCPFAGYF VEAHPSDHYI RSTNTKNDPD ALNALINKYS PNIKTWSPSP GAVLDLKKAI
QGDRDFITDP PRGTQKFKDS WDFEKYVNAI NKNIEEEIFS YPEWIQFYYK WTGFKNYNLV
IRMVERDDDF CPVVGGYDFM VDFVGEEPTF PTERPAREHS YLEMENRIGV HRETVRQGLF
WDDLYIGFNN RISREPDTFH YLFWNHMQIL LPRTDPDWEG FLRDMKTEGA PQKAIWNPSQ
ATPAVEAKDP SSDSKDSATK PGTHWNYERL LRPLGIVVAL VGVGVAIWKS ESK
