ID MBHL_OLICO Reviewed; 604 AA. AC O33406; Q6LB92; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 16-JUN-2009, entry version 54. DE RecName: Full=Uptake hydrogenase large subunit; DE EC=1.12.99.6; DE AltName: Full=Hydrogenlyase; DE AltName: Full=Membrane-bound hydrogenase large subunit; GN Name=hoxL; OrderedLocusNames=OCAR_p_08063; OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5). OG Plasmid megaplasmid pHCG3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=504832; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28. RX MEDLINE=97464431; PubMed=9324252; RA Santiago B., Meyer O.; RT "Purification and molecular characterization of the H2 uptake RT membrane-bound NiFe-hydrogenase from the carboxidotrophic bacterium RT Oligotropha carboxidovorans."; RL J. Bacteriol. 179:6053-6060(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14644498; DOI=10.1016/j.gene.2003.08.027; RA Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.; RT "Complete nucleotide sequence of the circular megaplasmid pHCG3 of RT Oligotropha carboxidovorans: function in the chemolithoautotrophic RT utilization of CO, H(2) and CO(2)."; RL Gene 322:67-75(2003). CC -!- FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to CC increase the production of ATP and to protect nitrogenase against CC inhibition or damage by O(2) under carbon- or phosphate-limited CC conditions (By similarity). CC -!- CATALYTIC ACTIVITY: H(2) + A = AH(2). CC -!- COFACTOR: Binds 1 nickel ion per subunit (By similarity). CC -!- SUBUNIT: Heterodimer of a large and a small subunit. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large CC subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X82447; CAG28467.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_015634.1; -. DR HSSP; P21852; 1UBL. DR GeneID; 2807125; -. DR GenomeReviews; X82447_GR; OCAR_p_08063. DR BRENDA; 1.12.99.6; 255922. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:EC. DR GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR Pfam; PF00374; NiFeSe_Hases; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. DR PROSITE; PS00508; NI_HGENASE_L_2; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Direct protein sequencing; Membrane; KW Metal-binding; Nickel; Oxidoreductase; Plasmid. FT INIT_MET 1 1 Removed. FT CHAIN 2 604 Uptake hydrogenase large subunit. FT /FTId=PRO_0000199714. FT METAL 76 76 Nickel (Potential). FT METAL 79 79 Nickel (Potential). FT METAL 583 583 Nickel (Potential). FT METAL 586 586 Nickel (Potential). SQ SEQUENCE 604 AA; 67144 MW; F4C5271D2B241535 CRC64; MSVIQTPNGY KLDNSGRRVV VDPVTRIEGH MRCEVNVDSN NVIRNAVSTG TMWRGLEVIL KGRDPRDAWA FVERICGVCT GCHALASVRA VENALDIRIP PNAHLIREIM AKVLQWHDHV VHFYHLHALD WVNPVNALKA DPKATSELQQ LVGPNHPMSS PGYFRDIQNR LKRFVESGEL GIFKNGYWDN PAYKLSPEAD LMATAHYLEA LDIQKEIVKI HTIFGGKNPH PNFMVGGVPC AINMDGDLAA GAPLNMERLN FVRARIEEAY EFSKNVYIPD VIAIATFYKG WLYGGGLSAT NVMDYGDYAK VNYDKSTDQL KGGAILNGNW NEVFPVDAAD PEQIQEFVAH SWYKYPDEAK GLHPWDGVTE HNYALGPNTK GTRTDIKQLD EAAKYSWIKS PRWRGHAVEV GPLSRYILNY AQGNQYVIEQ VDSSLAAFNK LAGTNLTPKQ ALPSTIGRTL ARALEAHYCA AMMLDDWKEL IGNIKAGDSS TANVEKWDPS TWPKEAKGYG LVAAPRGANG HWIRIKDGKI ANYQCIVPTT WNGSPRDPAG NIGAFEASLM NTPMERPEEP VEILRTLHSF DPCLACSTHV MSEDGENLAK VTVR //