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Database: UniProt
Entry: A3HRZ6_9BACT
LinkDB: A3HRZ6_9BACT
Original site: A3HRZ6_9BACT 
ID   A3HRZ6_9BACT            Unreviewed;       563 AA.
AC   A3HRZ6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00039545};
DE            EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE   AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00042773};
GN   ORFNames=ALPR1_10375 {ECO:0000313|EMBL:EAZ82614.1};
OS   Algoriphagus machipongonensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ82614.1, ECO:0000313|Proteomes:UP000003919};
RN   [1] {ECO:0000313|EMBL:EAZ82614.1, ECO:0000313|Proteomes:UP000003919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR1 {ECO:0000313|EMBL:EAZ82614.1,
RC   ECO:0000313|Proteomes:UP000003919};
RX   PubMed=21183675; DOI=10.1128/JB.01421-10;
RA   Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA   Fairclough S.R., King N.;
RT   "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT   colony-forming choanoflagellate.";
RL   J. Bacteriol. 193:1485-1486(2011).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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:EAZ82614.1}.
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DR   EMBL; AAXU02000001; EAZ82614.1; -; Genomic_DNA.
DR   RefSeq; WP_008200336.1; NZ_CM001023.1.
DR   AlphaFoldDB; A3HRZ6; -.
DR   STRING; 388413.ALPR1_10375; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_9_10; -.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000003919; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05936; FC-FACS_FadD_like; 1.
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:SF8; 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:EAZ82614.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003919}.
FT   DOMAIN          30..420
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          470..544
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   563 AA;  62382 MW;  8C1C6B06C2FC35BD CRC64;
     MQDFPWFKFY PKSVDKVVNC DAYGSVSELF EESVKKYGDS TAYECMGKTL SFNELDKLSS
     HFANYLIHVL KLEQGSRVAL QMPNTLQYPV AMFGALRAGM IVVNTNPLYT SAEMKHQFND
     AGADVIVIVA NFAHNLEKIR EEISAKRIII TELGDLLGFL KGTIVNLVVK HVKKMVPSYS
     LPGADTFKSA LEQGAEYEFH APKIKKSDTA FLQYTGGTTG VSKGAELSHG NIIANMQQIS
     EWMKPSLKER EEVVITALPL YHIFALTVNC LSMLKIGAHN VLITNPRDMP AFCKDLSKHK
     FSVFTGVNTL FNGLLNQESF KNLDFSHLKI AVGGGMAVQK STAEKWKKVT GTPLAEGYGL
     TETSPVASCN PIDGTERNGT IGIPLPNTEM CVMDDEGNML DIGERGEICI KGPQVMIGYW
     NRPKETAEVM RGEWFKSGDI GIMDEDGFFK IVDRKKEMIL VSGFNVYPNE IEDVIASCEG
     VLEVGVIGMP DPKSTEKVVA YVVPKGDSLS EDKVIAHCHE SLTNYKIPKE VYFTDELPKS
     NVGKILRRKI KEAHMEKIGA KTK
//
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