ID   CMAH_PIG                Reviewed;         435 AA.
AC   O19074;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
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;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ENZYME ACTIVITY.
RX   PubMed=8647250; DOI=10.1016/0014-5793(96)00384-5;
RA   Schlenzka W., Shaw L., Kelm S., Schmidt C.L., Bill E., Trautwein A.X.,
RA   Lottspeich F., Schauer R.;
RT   "CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-
RT   sulphur protein to be described in Eukarya.";
RL   FEBS Lett. 385:197-200(1996).
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:8647250}.
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:8647250};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
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; Y15010; CAA75243.1; -; mRNA.
DR   PIR; S68831; S68831.
DR   AlphaFoldDB; O19074; -.
DR   STRING; 9823.ENSSSCP00000001169; -.
DR   PaxDb; O19074; -.
DR   eggNOG; ENOG502QR0M; Eukaryota.
DR   BRENDA; 1.14.18.2; 6170.
DR   UniPathway; UPA00628; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR027033; Cnh.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR46522; PTHR46522; 1.
DR   SUPFAM; SSF56281; SSF56281; 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..435
FT                   /note="Cytidine monophosphate-N-acetylneuraminic acid
FT                   hydroxylase"
FT                   /id="PRO_0000127805"
FT   NON_TER         1
SQ   SEQUENCE   435 AA;  50628 MW;  5BE41630DF82908C CRC64;
     THACMDLKLG DKRMVFDPWL IGPAFARGWW LLHEPPSDWL ERLSRADLIY ISHMHSDHLS
     YPTLKKLAER RPDVPIYVGN TERPVFWNLN QSGVQLTNIN VVPFGIWQQV DKNLRFMILM
     DGVHPEMDTC IIVEYKGHKI LNTVDCTRPN GGRLPMKVAL MMSDFAGGAS GFPMTFSGGK
     FTEEWKAQFI KTERKKLLNY KARLVKDLQP RIYCPFPGYF VESHPADKYI KETNIKNDPN
     ELNNLIKKNS EVVTWTPRPG ATLDLGRMLK DPTDSKGIVE PPEGTKIYKD SWDFGPYLNI
     LNAAIGDEIF RHSSWIKEYF TWAGFKDYNL VVRMIETDED FSPLPGGYDY LVDFLDLSFP
     KERPSREHPY EEIRSRVDVI RHVVKNGLLW DDLYIGFQTR LQRDPDIYHH LFWNHFQIKL
     PLTPPDWKSF LMCSG