ID A0A0S2W1M9_9FIRM Unreviewed; 885 AA.
AC A0A0S2W1M9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN ORFNames=IB211_00865 {ECO:0000313|EMBL:ALP93259.1};
OS Intestinimonas butyriciproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP93259.1, ECO:0000313|Proteomes:UP000064844};
RN [1] {ECO:0000313|EMBL:ALP93259.1, ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|EMBL:ALP93259.1,
RC ECO:0000313|Proteomes:UP000064844};
RX PubMed=26620920; DOI=10.1038/ncomms10062;
RA Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT "Production of butyrate from lysine and the Amadori product fructoselysine
RT by a human gut commensal.";
RL Nat. Commun. 6:10062-10062(2015).
RN [2] {ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT "A butyrogenic pathway from the amino acid lysine in a human gut
RT commensal.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000256|ARBA:ARBA00024779, ECO:0000256|HAMAP-
CC Rule:MF_00036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001676, ECO:0000256|HAMAP-
CC Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000256|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00036}.
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DR EMBL; CP011307; ALP93259.1; -; Genomic_DNA.
DR RefSeq; WP_033116378.1; NZ_JPJD01000006.1.
DR AlphaFoldDB; A0A0S2W1M9; -.
DR STRING; 1297617.IB211_00865; -.
DR KEGG; ibu:IB211_00865; -.
DR PATRIC; fig|1297617.4.peg.879; -.
DR eggNOG; COG0013; Bacteria.
DR Proteomes; UP000064844; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00036};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Reference proteome {ECO:0000313|Proteomes:UP000064844};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Zinc {ECO:0000256|HAMAP-Rule:MF_00036}.
FT DOMAIN 6..716
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 885 AA; 97943 MW; 2DFA62B94BDFE81A CRC64;
MPTKKYGVNE LREMFLQFFE SKGHLRLPSF SLIPQNDASL LLINSGMAPM KPWFTGEQEP
PCHRVCTCQK CIRTGDIDNI GHTARHGTYF EMLGNFSFGD YFKHEAIAWS WEFLTSPEWV
GLDPERLYPS IYEEDDEAFE IWNKEIGIPA ERIFRFGKAD NFWEHGSGPC GPCSEIYYDR
GERYGCGRPD CTVGCDCDRY MEVWNNVFSQ FNNDGEGHYT ELKQKNIDTG MGLERLAVVC
QDVDSLFDVD TVMNITHKVT DITGARYGET REKDVSLRVI TDHIRSATFM ICDGVLPSNE
GRGYVLRRLL RRAARHGKLL GVNEPFLYEV CDTVIHENEG HYPELRERRD YITKVIRTEE
ENFARTIDGG MKIFNDLLAG HKGKGETVFS GADAFKLYDT YGFPIDLTIE MAAEQGLSVD
EEAFKALMQE QKERARKARE ALGDLGWAGV EFGKDVPETQ FVGYDHTSVD DARVAALVVE
NEQAEELMPG VEAIVVLDKT PFYAEMGGQV ADHGAITAPG GALFQVTDVQ KNKGGKYMHY
GKLTGGVLKL GDTVAAAIDV PRRKAVMRAH SATHLLDKAL RAVLGDHVQQ AGSLVEPDRL
RFDFTHFSAM TTEELQKVED MVNEAVLEGY EVCTDVLPIE EAKQRGAIAL FGEKYGDTVR
VVDMGHGYSV EFCGGTHLDN TAKVGVFHIL SEFSVASGVR RIEAITGHAT LACIRDNCCT
INAVSEALKT KPAELVQKAL QESQEIRELR HAVESFKAKE AVGEASNFLM GAREVGGLKV
LTATLNDAEA ERLRKMGDFL RDKDQRVVAV LSSVKDGKIT FLCVCGKEAV AKGIKAGDII
KKVTSLCGGK GGGKPDSAMG GGSDVLKLDN ALATVDDFVH EKLGL
//
