ID I0JQE9_HALH3 Unreviewed; 505 AA.
AC I0JQE9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:CCG46369.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:CCG46369.1};
GN OrderedLocusNames=HBHAL_4028 {ECO:0000313|EMBL:CCG46369.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG46369.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG46369.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
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DR EMBL; HE717023; CCG46369.1; -; Genomic_DNA.
DR RefSeq; WP_014644258.1; NC_017668.1.
DR AlphaFoldDB; I0JQE9; -.
DR STRING; 866895.HBHAL_4028; -.
DR KEGG; hhd:HBHAL_4028; -.
DR PATRIC; fig|866895.3.peg.3059; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_10_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF3; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CCG46369.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 9..367
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 417..492
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 505 AA; 56954 MW; AE1778DDE27965D6 CRC64;
MNLSELLAYQ SRKYPLKEGL ITPTSRLTYK EWNFKVNQFA HALRSLGIQP ADKVMIHMPN
TIEFVISYFA VHRVGAIAVP VNARLINSEL SYIFDHSDTT FFLTHELLFE QVTDLVHEKK
GTFIKTGSAT DYWLSFEELM SNESGTEIVN TAEEDTEASI LYTSGTTGKP KGVVFTHRNI
LTVSRMMAVE MEMKPSSRML HMMPLSHSAP LHLFMAAGTY VGAAHILAPS FSPELLLELA
SSERTTHFFG APVAYLLTAK HPKVTEIDLS WMKYWVYGGA PLSRSEVQFI QEQLDTEQLY
CVYGLTEAGP NGSLLLPLEH DEKAGSIGQR AALNCEMKVV DDQGNEAGID EVGEIILRGE
GTMKGYYKDE VKTKEALKDG WLYTGDLAQR DQDGFYWVVD RKKDIIISGG SNVYPREIED
ALLRHPHVQD VAVIGVPHPD WGETVKAFIV QDGTMNHLAE ECKEYLRQEI ADYKIPKLYE
EISELPRNAT GKLMKNQLRD QIHNR
//
