ID Q6PC06_DANRE Unreviewed; 591 AA.
AC Q6PC06; A0A8M1PCF8; F1QFK1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN Name=ahcyl2b {ECO:0000313|Ensembl:ENSDARP00000111142,
GN ECO:0000313|RefSeq:NP_958497.1, ECO:0000313|ZFIN:ZDB-GENE-040115-5};
GN Synonyms=ahcyl2 {ECO:0000313|RefSeq:NP_958497.1};
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:0000313|EMBL:AAH59517.1};
RN [1] {ECO:0000313|EMBL:AAH59517.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Wild-type {ECO:0000313|EMBL:AAH59517.1};
RC TISSUE=Eye {ECO:0000313|EMBL:AAH59517.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_958497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_958497.1};
RX PubMed=16754674; DOI=10.1074/jbc.M602520200;
RA Cooper B.J., Key B., Carter A., Angel N.Z., Hart D.N., Kato M.;
RT "Suppression and overexpression of adenosylhomocysteine hydrolase-like
RT protein 1 (AHCYL1) influences zebrafish embryo development: a possible role
RT for AHCYL1 in inositol phospholipid signaling.";
RL J. Biol. Chem. 281:22471-22484(2006).
RN [3] {ECO:0000313|RefSeq:NP_958497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_958497.1};
RX PubMed=21205313;
RA Mirbahai L., Williams T.D., Zhan H., Gong Z., Chipman J.K.;
RT "Comprehensive profiling of zebrafish hepatic proximal promoter CpG island
RT methylation and its modification during chemical carcinogenesis.";
RL BMC Genomics 12:3-3(2011).
RN [4] {ECO:0000313|Ensembl:ENSDARP00000111142}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000111142};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSDARP00000111142, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000111142};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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).
RN [6] {ECO:0000313|RefSeq:NP_958497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_958497.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [7] {ECO:0000313|RefSeq:NP_958497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_958497.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [8] {ECO:0000313|RefSeq:NP_958497.1}
RP IDENTIFICATION.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_958497.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC Evidence={ECO:0000256|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU000548};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|RuleBase:RU000548}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
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DR EMBL; CU468915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059517; AAH59517.1; -; mRNA.
DR RefSeq; NP_958497.1; NM_201340.1.
DR STRING; 7955.ENSDARP00000111142; -.
DR PaxDb; 7955-ENSDARP00000111142; -.
DR Ensembl; ENSDART00000130453.4; ENSDARP00000111142.2; ENSDARG00000039343.9.
DR GeneID; 394240; -.
DR KEGG; dre:394240; -.
DR AGR; ZFIN:ZDB-GENE-040115-5; -.
DR CTD; 394240; -.
DR ZFIN; ZDB-GENE-040115-5; ahcyl2b.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_1_1; -.
DR OMA; HIIWPDA; -.
DR OrthoDB; 120477at2759; -.
DR TreeFam; TF300415; -.
DR Reactome; R-DRE-425381; Bicarbonate transporters.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000039343; Expressed in intestine and 39 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR NCBIfam; TIGR00936; ahcY; 1.
DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF2; ADENOSYLHOMOCYSTEINASE 3; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:AAH59517.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU000548};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000548};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q6PC06};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 350..511
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 15..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 65087 MW; 6D916B5342EA7D15 CRC64;
MSVQAVATKM AEVELKDVAG KDSPPAISPL TPKAEEKKTE INSSSTSMAA AAAVDPSPVT
VAPSPMKMPQ ASAMKRTDPQ QNGGEAFVNC DGTVAEGPRM KKIQFADQKQ EFNKRPTKIG
RRSLSRSISQ SSTDSYSSAA SYTDSSDDET SPRDKQQKNS KGSGDFCIKN IKQADFGRRE
IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA VLMETLSALG AQCRWAACNI
YSTQNEVAAA LAEGGFSVFA WKGESEDDFW WCIDRCVNVE GWQPNMILDD GGDLTHWIYK
KYPNMFKKIK GIVEESVTGV HRLYQLSKAG KLCVPAMNVN DSVTKQKFDN LYCCRESILD
GLKRTTDVMF GGKQVVVCGY GEVGKGCSAA LKAMGSIVYV TEIDPICALQ ACMDGFRLVK
LSEVIRQVDI VITCTGNKNV VVREYMDRMK NGCIVCNMGH SNTEIDVASL RTPELTWERV
RSQVDHVIWP DGKRIVLLAE GRLLNLSCST VPTFVLSITA TTQALALIEL YNAPEGRYKQ
DVYLLPKKMD EYVASLHLPT FDAHLTELSD EQAKYLGLNK NGPFKPNYYR Y
//
