NEUAB_DANRE
ID NEUAB_DANRE Reviewed; 423 AA.
AC H9BFW7; E7F0X7;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=N-acylneuraminate cytidylyltransferase B {ECO:0000305|PubMed:22351762};
DE EC=2.7.7.43 {ECO:0000269|PubMed:22351762};
DE AltName: Full=CMP-sialic acid synthetase 2 {ECO:0000303|PubMed:22351762};
GN Name=cmasb {ECO:0000312|ZFIN:ZDB-GENE-120427-1};
GN Synonyms=cmas2 {ECO:0000303|PubMed:22351762};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AFC17881.1};
RN [1] {ECO:0000312|EMBL:AFC17881.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PATHWAY, SUBUNIT,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 179-PRO--ARG-182.
RX PubMed=22351762; DOI=10.1074/jbc.m111.327544;
RA Schaper W., Bentrop J., Ustinova J., Blume L., Kats E., Tiralongo J.,
RA Weinhold B., Bastmeyer M., Munster-Kuhnel A.K.;
RT "Identification and biochemical characterization of two functional CMP-
RT sialic acid synthetases in Danio rerio.";
RL J. Biol. Chem. 287:13239-13248(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Catalyzes the activation of 2-keto-3-deoxy-D-glycero-D-
CC galacto-nononic acid (KDN) to cytidine 5'-monophosphate 2-keto-3-deoxy-
CC D-glycero-D-galacto-nononic acid (CMP-KDN), a substrate required for
CC the addition of sialic acid. Also has weak activity towards N-
CC acetylneuraminic acid (NeuNAc) and N-glycolylneuraminic acid (Neu5Gc).
CC {ECO:0000269|PubMed:22351762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate +
CC diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43;
CC Evidence={ECO:0000269|PubMed:22351762};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC {ECO:0000269|PubMed:22351762}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22351762}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22351762}.
CC -!- DEVELOPMENTAL STAGE: During early stages of development (9-18 hours
CC post fertilization, hpf) has weak and ubiquitous expression. Expression
CC is restricted to brain at 24 hpf. At the hatching stage (48 hpf),
CC detected in heart but not in brain. {ECO:0000269|PubMed:22351762}.
CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR EMBL; JQ015187; AFC17881.1; -; mRNA.
DR EMBL; CABZ01039863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001245338.1; NM_001258409.1.
DR AlphaFoldDB; H9BFW7; -.
DR SMR; H9BFW7; -.
DR STRING; 7955.ENSDARP00000107758; -.
DR GeneID; 100885772; -.
DR KEGG; dre:100885772; -.
DR CTD; 100885772; -.
DR ZFIN; ZDB-GENE-120427-1; cmasb.
DR eggNOG; ENOG502QQH3; Eukaryota.
DR OrthoDB; 781897at2759; -.
DR BRENDA; 2.7.7.43; 928.
DR UniPathway; UPA00628; -.
DR PRO; PR:H9BFW7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IDA:ZFIN.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..423
FT /note="N-acylneuraminate cytidylyltransferase B"
FT /id="PRO_0000438686"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT MUTAGEN 179..181
FT /note="Missing: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22351762"
SQ SEQUENCE 423 AA; 47665 MW; C58DAC33164DB9CF CRC64;
MEGGRCAQVS SVPASPSSGH RHRAALILAR GGSKGIPLKN IKNLAGVPLI GWVLRAALDS
DVDSVWVSTD HDEIERVAKL WGAKVHRRSP EVSKDSSSSL ETIQEFIRLR PEVDVICHIQ
ATSPCLHPHH INEALQKITH QGFSYVLSVV RRHQFRWEEL QENEDRNPKS FNINVAQRPR
RQDWPGELYE NGSFYFSTRK AWESGLTELG RIAYYEMPPE FSVDIDVDID WPVAEQRVLR
FGYFGREENA AVRLFLCKVS GCLTNGQIYM SVSGEDLVTI NARDVAGIQM LQKENIEVIL
ISSVNEPLSR GVLEKVSQRA GCGLSFTEQR NALEMQKLMD KRKLHWDQVA FMGSESEDVE
IMSQAGLNGV PSDAPVAELI AAKYTCQRAG GHGAVREFAE YILSMKRKSS REENHERIDK
HNF
