GenomeNet

Database: UniProt
Entry: G1LF26_AILME
LinkDB: G1LF26_AILME
Original site: G1LF26_AILME 
ID   G1LF26_AILME            Unreviewed;       334 AA.
AC   G1LF26;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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:ENSAMEP00000005513.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000005513.1, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000005513.1, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000005513.1}
RP   IDENTIFICATION.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_002926826.1; XM_002926780.3.
DR   AlphaFoldDB; G1LF26; -.
DR   STRING; 9646.ENSAMEP00000005513; -.
DR   Ensembl; ENSAMET00000005739.2; ENSAMEP00000005513.1; ENSAMEG00000005210.2.
DR   GeneID; 100481953; -.
DR   CTD; 27430; -.
DR   eggNOG; KOG1430; Eukaryota.
DR   GeneTree; ENSGT00390000006721; -.
DR   HOGENOM; CLU_045518_0_0_1; -.
DR   InParanoid; G1LF26; -.
DR   OMA; IRTAWVY; -.
DR   OrthoDB; 3080056at2759; -.
DR   TreeFam; TF332849; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
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:UP000008912}.
FT   DOMAIN          30..322
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   334 AA;  37673 MW;  149FC8E0B9DE5A57 CRC64;
     MVGRENELSI HFVPGSCRLV EEEVNVPNRR VLITGATGLL GRAVYKEFKQ NNWHAFGCGF
     RRARPKFEQV NLLDSEAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL
     AKEAASIGAF LIYISSDYVF DGTNPPYREE DVPSPLNLYG KTKLEGEKAV LENNLGAAVL
     RIPVLYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML
     DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCTKL
     ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH
//
DBGET integrated database retrieval system