ID Z9JWC4_9MICO Unreviewed; 902 AA.
AC Z9JWC4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=BF93_06535 {ECO:0000313|EMBL:EWS82680.1};
OS Brachybacterium phenoliresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS82680.1, ECO:0000313|Proteomes:UP000023067};
RN [1] {ECO:0000313|EMBL:EWS82680.1, ECO:0000313|Proteomes:UP000023067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS82680.1,
RC ECO:0000313|Proteomes:UP000023067};
RA Wang X.;
RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL Submitted (FEB-2014) 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|HAMAP-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|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWS82680.1}.
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DR EMBL; JDYK01000002; EWS82680.1; -; Genomic_DNA.
DR RefSeq; WP_038370159.1; NZ_KK069988.1.
DR AlphaFoldDB; Z9JWC4; -.
DR STRING; 396014.BF93_06535; -.
DR PATRIC; fig|396014.3.peg.300; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_11; -.
DR OrthoDB; 9803884at2; -.
DR Proteomes; UP000023067; Unassembled WGS sequence.
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: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 Gene3D; 6.10.250.550; -; 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:UP000023067};
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 1..728
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 902 AA; 96891 MW; A363EE30F8304390 CRC64;
MRTAEIQRRF LDFFEKKGHA AVPSASLVSS DPSILFTIAG MVPFIPYIVG TEKAPWPRAA
SVQKCIRTND IENVGRTTRH GTFFQMAGNF SFGDYFKAGA IDFSWELLTS SQDEGGFGLD
PQRLWITLWE EDQESYTHLT EVIGLDPARI VQLPWEESCW DTGQPGPAGS TGEWYYDRGP
DYGPDAPSGR QAQWPGDERA EDRYLEIWNL VFDQFLRGPG AGKDYELLGE LDDKAIDTGL
GVERLAYLLQ DKQNMYETDQ VFPVIERTQQ LTGRTYGADA EDDVRMRVVA DHVRSAMMLA
SDGVRPGNEG RGYVMRRLIR RAVRSVRLLG YDRPAMPELL PVSLTAMQEA YPSLEADAER
IREVIYAEED AFRRTLVTGS AIFDQVAEEV RASGGRSVSG ADAFRLHDTY GFPIDLTLEM
AQEVGLSVDE GGFRSAMQEQ RERARADAAA KKGGHADTAV YNRLLGERGE AVPFLGYTDH
TVSTTVESVL VDGALVDAVD APAEVEIVLA ATPFYAEMGG QLADQGRIAL NNGGIVEVDD
VQSPVKGLIV HRGRLVEGTA AAGVGAIAEI DLERRGAIAR AHTATHMVHQ ALREELGDGA
TQAGSENSPG RMRFDFRYGQ GVPRSSLEQI EGRVNTQLQQ ELLVTDQQMP LEEARAAGAM
ALFGEKYPEI VRVVSIGGDW SKELCAGTHV ATTGAIGTVQ LMGESSIGSG VRRVDALVGL
SAYRFQAKEH ALVSQLTELL KVGSAEDLPE RVRGLAQRVK DMEKQLAALR GAQLQAQAGE
LAGSARDAGG VRLLVHDAGE GVAAGDLRTL VTDLRSRLGE DAPSVVAVTG SVDGKAALVV
ATNASAREKG LRAGALLRAG AEAMGGRGGG KDDLAQGGGG DSARTAQALD AVAAAVTVAA
SA
//
