ID   MAT2B_DANRE             Reviewed;         323 AA.
AC   Q5BJJ6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE   AltName: Full=Methionine adenosyltransferase II beta;
DE            Short=MAT II beta;
GN   Name=mat2b; ORFNames=zgc:110308;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an
CC       enzyme that catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. Regulates MAT2A catalytic activity by changing its
CC       kinetic properties, increasing its affinity for L-methionine. Can bind
CC       NADP (in vitro). {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- SUBUNIT: Heterotrimer; composed of a catalytic mat2a homodimer that
CC       binds one regulatory mat2b chain. Heterohexamer; composed of a central,
CC       catalytic mat2a homotetramer flanked on either side by a regulatory
CC       mat2b chain. NADP binding increases the affinity for mat2a.
CC       {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       MAT2B subfamily. {ECO:0000305}.
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DR   EMBL; BC091455; AAH91455.1; -; mRNA.
DR   AlphaFoldDB; Q5BJJ6; -.
DR   SMR; Q5BJJ6; -.
DR   STRING; 7955.ENSDARP00000123222; -.
DR   PaxDb; Q5BJJ6; -.
DR   DNASU; 541347; -.
DR   ZFIN; ZDB-GENE-030131-786; mat2b.
DR   eggNOG; KOG1430; Eukaryota.
DR   InParanoid; Q5BJJ6; -.
DR   PhylomeDB; Q5BJJ6; -.
DR   Reactome; R-DRE-156581; Methylation.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   UniPathway; UPA00315; UER00080.
DR   PRO; PR:Q5BJJ6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0048269; C:methionine adenosyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0048270; F:methionine adenosyltransferase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; PTHR10491; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; One-carbon metabolism; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Methionine adenosyltransferase 2 subunit beta"
FT                   /id="PRO_0000287524"
FT   REGION          308..323
FT                   /note="Required for interaction with MAT2A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         26..29
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         49..51
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         60..61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         146
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         172
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
SQ   SEQUENCE   323 AA;  36359 MW;  4B7B73191895ACE6 CRC64;
     MPGFNYGGDQ DEVYTPYRRV LVTGATGLLG RAVYKEFKNN DWDALGCGYN RARPFFLKCN
     LLDEDAVRGV IQSFQPHVIV HCAAERRPDV VERHTEAAMN LNVHACATLA KEAGGSFLIY
     ISTDYVFDGR NPPYGENDAP NPLNLYGKSK LEGEREILRH CPGAAVLRVP ILFGEVEKVE
     ESAVTVLFER VQEGAESCTI DHCQQRFPTY TNDVARVCRN MAERALQDQS LRGIFHYSAK
     EQMTKYEMTC AIADAFNLPS SHLIPMTEQP AGAGAQRPQN AQLECSRLEL LGLSVESTPF
     KNAIRDSLWP FQHDKRWRQT VFH