ID A0A286XHH0_CAVPO Unreviewed; 334 AA.
AC A0A286XHH0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Methionine adenosyltransferase 2 subunit beta {ECO:0000256|ARBA:ARBA00021596, ECO:0000256|RuleBase:RU364081};
DE AltName: Full=Methionine adenosyltransferase II beta {ECO:0000256|ARBA:ARBA00029977, ECO:0000256|RuleBase:RU364081};
GN Name=MAT2B {ECO:0000313|Ensembl:ENSCPOP00000024791.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000024791.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000024791.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000024791.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU364081}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005224, ECO:0000256|RuleBase:RU364081}.
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:0000256|RuleBase:RU364081}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC MAT2B subfamily. {ECO:0000256|ARBA:ARBA00008656,
CC ECO:0000256|RuleBase:RU364081}.
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DR EMBL; AAKN02022688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003473224.1; XM_003473176.3.
DR AlphaFoldDB; A0A286XHH0; -.
DR STRING; 10141.ENSCPOP00000024791; -.
DR Ensembl; ENSCPOT00000037323.1; ENSCPOP00000024791.1; ENSCPOG00000002033.4.
DR GeneID; 100733146; -.
DR KEGG; cpoc:100733146; -.
DR CTD; 27430; -.
DR VEuPathDB; HostDB:ENSCPOG00000002033; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00390000006721; -.
DR InParanoid; A0A286XHH0; -.
DR OMA; IRTAWVY; -.
DR OrthoDB; 3080056at2759; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000002033; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; IEA:Ensembl.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU364081};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 30..322
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 334 AA; 37568 MW; 165222266436230D CRC64;
MVGREKELSI HFVPGCCRLV EEEVNVPSRR VLVTGATGLL GRAVYKEFQQ NNWHAVGCGF
RRARPKFEQV NLLDSEAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL
AKEAAAVGAF LIYISSDYVF DGTNPPYREE DIPAPLNLYG KTKLEGEKAV LENNLGAAVL
RIPVLYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML
DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL
ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH
//
