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Database: UniProt
Entry: A0A093H7L2_STRCA
LinkDB: A0A093H7L2_STRCA
Original site: A0A093H7L2_STRCA 
ID   A0A093H7L2_STRCA        Unreviewed;       313 AA.
AC   A0A093H7L2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 18.
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};
DE   Flags: Fragment;
GN   ORFNames=N308_13118 {ECO:0000313|EMBL:KFV75365.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV75365.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV75365.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV75365.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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.
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; KL205832; KFV75365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093H7L2; -.
DR   STRING; 441894.ENSSCUP00000006708; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000053584};
KW   Transferase {ECO:0000313|EMBL:KFV75365.1}.
FT   DOMAIN          9..301
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV75365.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:KFV75365.1"
SQ   SEQUENCE   313 AA;  34925 MW;  71EFC822C81DA11D CRC64;
     EDVDIPSRRV LITGATGLLG RAVFKEFNGN NWNAVGCGYR RAQPRFEQIN LLDSIAVHDI
     IHDFQPHVIV HCAAERRPDV VESQPDAASQ LNVAASGNLA KEAAGIGAFL VYISTDYVFD
     GTSPPYKETD APNPLNLYGK TKLEGEKAVL ENNEDAAVLR VPILYGEVER LEESAVTVMF
     DKVQFSNKSA NMDHWQQRFP TNVKDVAAVC RQLAEKRMLD PSVKGIFHWS GNEQMTKYEM
     ACAIADAFNL PSSHLRPITD CPVLGALRPR NAQLDCSKLE MLGIGQRTSF RAGIKESLWP
     FLVDKRWRQT VFH
//
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