ID Q5F3Q3_CHICK Unreviewed; 540 AA.
AC Q5F3Q3;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 08-NOV-2023, entry version 106.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
GN ORFNames=RCJMB04_10b17 {ECO:0000313|EMBL:CAH65231.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAH65231.1};
RN [1] {ECO:0000313|EMBL:CAH65231.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB {ECO:0000313|EMBL:CAH65231.1};
RC TISSUE=Bursa {ECO:0000313|EMBL:CAH65231.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122}.
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DR EMBL; AJ851597; CAH65231.1; -; mRNA.
DR RefSeq; NP_001026084.1; NM_001030913.1.
DR AlphaFoldDB; Q5F3Q3; -.
DR KEGG; gga:419803; -.
DR VEuPathDB; HostDB:geneid_419803; -.
DR PhylomeDB; Q5F3Q3; -.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
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 PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF3; S-ADENOSYLHOMOCYSTEINE HYDROLASE-LIKE PROTEIN 1; 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 2: Evidence at transcript level;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT DOMAIN 285..446
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 59231 MW; 66E479BFA2368F92 CRC64;
MSVPEPAGGE EAKQAKEAED AEKFSFMATV TKAPKKQIQF ADDMQEFTKF PTKTGRRSLS
RSISQSSTDS YSSAASYTDS SDDEVSPREK QQTNSKGSSN FCVKNIKQAE FGRREIEIAE
QDMSALISLR KRAQGEKPLA GAKIVGCTHI TAQTAVLIET LCALGAQCRW SACNIYSTQN
EVAAALAEAG VAVFAWKGES EDDFWWCIDR CVNVDGWQAN MILDDGGDLT HWVYKKYPNI
FKKIRGIVEE SVTGVHRLYQ LSKAGKLCVP AMNVNDSVTK QKFDNLYCCR ESILDGLKRT
TDVMFGGKQV AVCGYGEVGK GCCAALKALG AIVYVTEIDP ICALQACMDG FRVVKLSEVI
RQVDVVITCT GNKNVVTREH LDRMKNSCIV CNMGHSNTEI DVTSLRTPEL TWERVRSQVD
HVIWPDGKRV VLLAEGRLLN LSCSTVPTFV LSITATTQAL ALIELYNAPE GRYKQDVYLL
PKKMGSRFSS PFWGTGLHRV QSASTASQAL LLLLCDESPS LSCSQMSTLP ACTCLPSTPT
//
