ID   MAT2B_XENTR             Reviewed;         334 AA.
AC   Q566L8; Q07G14;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE   AltName: Full=Methionine adenosyltransferase II beta;
DE            Short=MAT II beta;
GN   Name=mat2b; ORFNames=TEgg038m14.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-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; CR855516; CAL49345.1; -; mRNA.
DR   EMBL; BC093462; AAH93462.1; -; mRNA.
DR   RefSeq; NP_001016828.2; NM_001016828.3.
DR   AlphaFoldDB; Q566L8; -.
DR   SMR; Q566L8; -.
DR   PaxDb; Q566L8; -.
DR   DNASU; 549582; -.
DR   GeneID; 549582; -.
DR   KEGG; xtr:549582; -.
DR   CTD; 27430; -.
DR   Xenbase; XB-GENE-972023; mat2b.
DR   eggNOG; KOG1430; Eukaryota.
DR   InParanoid; Q566L8; -.
DR   OrthoDB; 1007850at2759; -.
DR   Reactome; R-XTR-156581; Methylation.
DR   Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000015071; Expressed in egg cell and 12 other tissues.
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..334
FT                   /note="Methionine adenosyltransferase 2 subunit beta"
FT                   /id="PRO_0000287526"
FT   REGION          319..334
FT                   /note="Required for interaction with MAT2A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         37..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         60..62
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         71..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         159
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         185
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   CONFLICT        52
FT                   /note="S -> N (in Ref. 1; CAL49345)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="V -> I (in Ref. 1; CAL49345)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  37804 MW;  6455EBC29E2FD702 CRC64;
     MEGRHKEYRI RFSPGWVEVV QDDVTIPGRR ALITGATGLL GRAVYKEFKE NSWHVLGCGY
     SRARPRFEYL NLLDAAAVKA LIQDFKPHVI IHCAAERRPD IVESQPEFAS LLNVVASENL
     AKEAAGVGAF LIYVSSDYVF DGTSPPYRED SVPNPLNLYG KTKLEGERAV LHNNEGAAVL
     RVPVLYGDVE KLSESAVTIL FDKVQFSNKS ANMDHWQQRF PTYVKDVASV CLQLTERRLQ
     DPSIKGIYHW SGNEQMTKYE MTCAMADAFN LPSSHLRPIT DEPVGATPRP WNPQLDCSKL
     EKIGIGQRTP FRVGIRESLW PFLVDKRWRQ TVFH