ID   MAT2B_BOVIN             Reviewed;         334 AA.
AC   Q29RI9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE   AltName: Full=Methionine adenosyltransferase II beta;
DE            Short=MAT II beta;
GN   Name=MAT2B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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; BC114151; AAI14152.1; -; mRNA.
DR   RefSeq; NP_001039991.1; NM_001046526.2.
DR   AlphaFoldDB; Q29RI9; -.
DR   SMR; Q29RI9; -.
DR   STRING; 9913.ENSBTAP00000016399; -.
DR   PaxDb; Q29RI9; -.
DR   PRIDE; Q29RI9; -.
DR   Ensembl; ENSBTAT00000016399; ENSBTAP00000016399; ENSBTAG00000012350.
DR   GeneID; 614177; -.
DR   KEGG; bta:614177; -.
DR   CTD; 27430; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012350; -.
DR   VGNC; VGNC:31262; MAT2B.
DR   eggNOG; KOG1430; Eukaryota.
DR   GeneTree; ENSGT00390000006721; -.
DR   HOGENOM; CLU_045518_0_0_1; -.
DR   InParanoid; Q29RI9; -.
DR   OMA; RMPLMFG; -.
DR   OrthoDB; 1007850at2759; -.
DR   TreeFam; TF332849; -.
DR   Reactome; R-BTA-156581; Methylation.
DR   Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000012350; Expressed in oocyte and 105 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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Methionine adenosyltransferase 2 subunit beta"
FT                   /id="PRO_0000287519"
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   MOD_RES         309
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
SQ   SEQUENCE   334 AA;  37768 MW;  8A1A91335E6D65BF CRC64;
     MVGREKELSI HFVPGDCRLV EEEVNIPNRR VLITGATGLL GRAVYKEFQQ NNWHAVGCGF
     RRARPKFEQV NLLDSNAVHH IIYDFQPHVI VHCAAERRPD VVENHPDAAS QLNVDASGNL
     AKEAAAIGAF LIYISSDYVF DGTNPPYREE DIPNPLNLYG KTKLEGEKAV LENNLGAAVL
     RIPVLYGEVE RLEESAVTIM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML
     DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVVGAQRP RNAQLDCSRL
     ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH