ID   MAT2B_RAT               Reviewed;         334 AA.
AC   Q5U2R0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE   AltName: Full=Methionine adenosyltransferase II beta;
DE            Short=MAT II beta;
GN   Name=Mat2b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC085899; AAH85899.1; -; mRNA.
DR   RefSeq; NP_001037747.1; NM_001044282.1.
DR   AlphaFoldDB; Q5U2R0; -.
DR   SMR; Q5U2R0; -.
DR   BioGRID; 598531; 1.
DR   STRING; 10116.ENSRNOP00000004269; -.
DR   jPOST; Q5U2R0; -.
DR   PaxDb; Q5U2R0; -.
DR   PRIDE; Q5U2R0; -.
DR   GeneID; 683630; -.
DR   KEGG; rno:683630; -.
DR   CTD; 27430; -.
DR   RGD; 1593534; Mat2b.
DR   VEuPathDB; HostDB:ENSRNOG00000003177; -.
DR   eggNOG; KOG1430; Eukaryota.
DR   HOGENOM; CLU_045518_0_0_1; -.
DR   InParanoid; Q5U2R0; -.
DR   OMA; AGETTWH; -.
DR   OrthoDB; 1007850at2759; -.
DR   PhylomeDB; Q5U2R0; -.
DR   Reactome; R-RNO-156581; Methylation.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   SABIO-RK; Q5U2R0; -.
DR   UniPathway; UPA00315; UER00080.
DR   PRO; PR:Q5U2R0; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003177; Expressed in frontal cortex and 20 other tissues.
DR   ExpressionAtlas; Q5U2R0; baseline and differential.
DR   Genevisible; Q5U2R0; RN.
DR   GO; GO:0048269; C:methionine adenosyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
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_0000287523"
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;  37375 MW;  FA65863830981734 CRC64;
     MVGREKELSI HFVPGCCQLV EEEVNIPSRR VLITGATGLL GRAVYKEFQQ SNWHAVGCGF
     RRARPKFEQV NLLDSEAVHH LIHDFQPHVI VHCAAERRPD VVESQPDAAS QLNVGASGNL
     AKEAAAIGAF LIYISSDYVF DGTNPPYTEE DIPSPLNLYG KTKLDGEKAV LENNLGAAVL
     RIPVLYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVASV CRQLAEKRML
     DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVIGAQRP KNAQLDCSKL
     ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH