ID A0A1H7KD79_RUMAL Unreviewed; 336 AA. AC A0A1H7KD79; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 16-JAN-2019, entry version 8. DE RecName: Full=Aspartate--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964848}; DE EC=6.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964843}; DE AltName: Full=Asparagine synthetase A {ECO:0000256|HAMAP-Rule:MF_00555}; GN Name=asnA {ECO:0000256|HAMAP-Rule:MF_00555}; GN ORFNames=SAMN05216469_106170 {ECO:0000313|EMBL:SEK84712.1}; OS Ruminococcus albus. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=1264 {ECO:0000313|EMBL:SEK84712.1, ECO:0000313|Proteomes:UP000186015}; RN [1] {ECO:0000313|EMBL:SEK84712.1, ECO:0000313|Proteomes:UP000186015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH2T6 {ECO:0000313|EMBL:SEK84712.1, RC ECO:0000313|Proteomes:UP000186015}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + CC L-asparagine; Xref=Rhea:RHEA:11372, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:456215; CC EC=6.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00555, CC ECO:0000256|SAAS:SAAS01124561}; CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L- CC asparagine from L-aspartate (ammonia route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00555, ECO:0000256|SAAS:SAAS00964853}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00555, CC ECO:0000256|SAAS:SAAS00964846}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. AsnA subfamily. {ECO:0000256|HAMAP-Rule:MF_00555, CC ECO:0000256|SAAS:SAAS00964852}. 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 EMBL; FOAT01000006; SEK84712.1; -; Genomic_DNA. DR RefSeq; WP_074832823.1; NZ_FOAT01000006.1. DR UniPathway; UPA00134; UER00194. DR Proteomes; UP000186015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00555; AsnA; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004618; AsnA. DR PANTHER; PTHR30073; PTHR30073; 1. DR Pfam; PF03590; AsnA; 1. DR PIRSF; PIRSF001555; Asp_ammon_ligase; 1. DR TIGRFAMs; TIGR00669; asnA; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964850}; KW Asparagine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964847}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964849}; KW Complete proteome {ECO:0000313|Proteomes:UP000186015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964845}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964851, ECO:0000313|EMBL:SEK84712.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00555, KW ECO:0000256|SAAS:SAAS00964844}. FT DOMAIN 25 321 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. SQ SEQUENCE 336 AA; 38618 MW; BE227B0E8DB516A6 CRC64; MSKSLYLPEG YTPALSLRET QHAIKYIKDV FQQALSIQLM LDRVSAPLIV RHGSGINDDL NGVERKVNFD IKEIDGEAEV VQSLAKWKRM ALYRYGYQAG EGIYTDMNAI RRDDDTDNLH SIFVDQWDWE KVIRREQRTE EFLKDTVKCV VKAIVYTKRK VSLRYPQLKN TVSEDVFFIT TQELEDMYPD KTSKEREKLI TKEHKTVFIM KIGGKLKSGE KHDGRAPDYD DWSLNGDIFF WDEVLDNAIE ISSMGIRVDE KSLASQLKEA DAEDRMQYDY HKMIANGTLP LTIGGGIGQS RLCMFLLEKA HIGEVQSSIW PEDMIEKCAA KGITLL //