ID A0A1Q2HLB4_9BACT Unreviewed; 1067 AA.
AC A0A1Q2HLB4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NADP-reducing hydrogenase subunit HndC {ECO:0000313|EMBL:AQQ08257.1};
DE EC=1.12.1.3 {ECO:0000313|EMBL:AQQ08257.1};
GN Name=hndC_1 {ECO:0000313|EMBL:AQQ08257.1};
GN ORFNames=L21SP3_00033 {ECO:0000313|EMBL:AQQ08257.1};
OS Sedimentisphaera cyanobacteriorum.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1940790 {ECO:0000313|EMBL:AQQ08257.1, ECO:0000313|Proteomes:UP000188273};
RN [1] {ECO:0000313|Proteomes:UP000188273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D3 {ECO:0000313|Proteomes:UP000188273};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP019633; AQQ08257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HLB4; -.
DR STRING; 1940790.L21SP3_00033; -.
DR KEGG; pbu:L21SP3_00033; -.
DR OrthoDB; 9778740at2; -.
DR Proteomes; UP000188273; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF10531; SLBB; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:AQQ08257.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 465..510
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 1067 AA; 116241 MW; F9B8BEE1C96E59C0 CRC64;
MDEIKKFNSL EEFKKISEQL RESSTQPGDT EKIFICTGGG CIASGALNLR DELKSCLQAN
GLSEKVQVVE TGCMGPCSAG PVLLMGRDKT FYVQVQPDDA EEIVQSHIMQ NKLVERLCWR
DEKTDKPAAS KLDIEFFKKQ TKIALRNCGL ITPTDLRASI SVGGFDGLAA VLAGISRDEV
IEQLKDSGLR GRGGAGFPTH MKWTFTKKSP GEVKYVVCNA DEGDPGAFMD RSVLEGDPYS
LIEGMSIAAY TIGAQRGFVY VRAEYPLAIE RLSESIEKCY KAGLLGENIL GTDFSFDLEI
RKGSGAFVCG EETALMASIE GKRGEPRPRP PFPAQKGLWD KPTVLNNVET YANVAAIVAK
GGKWFASFGT EKSRGTKVFA LAGAIRNSGL VEVPIGTTLG DLIYDIGGGI PNGKAFKAAQ
IGGPSGGCVP LQHLNVSLDY ESLNKLGAVM GSGGLVVMDE DTCMVDVARF FLEFVQEESC
GKCIPCRVGT KRMLEILDKI CSGQGEQGDI ERLEALGEKI RDTALCGLGQ TAPNPVLSTV
RHFRDEYEAH IIDKHCPAGV CPDMVLAPCK SACPAGVNIP GFVSLVGEER YAEALRLHRE
RNPFAAVCAR VCFHTCEEKC RRSSLDEPVS IRGVKRFMVD QEIVAQIPEV HENDENAKRK
IAVIGAGPSG FSCAYFLARL GYKPTVFEAR SRPGGMLVQA IPEYRLPKEI IAREYRMIQG
MGVKLVTDSK LGKDFTLQQL REQGYEAVYL AIGQPDGVML NMAGSDAEGV KEALDFLREY
NMKGSVEAGK NVAIIGGGNS AIDAARTAVR LGANVTVVYR RTQSEMPAYA EEIEESQQEG
VRIIELASPE RIVTENGRVS GLKCKKMKLG DYDASGRKKP VASGEEFTLD ADQVIFAVGQ
TMNLEPIFGK VINPQGETGY EYFVEVGNEK LRLNGKSKIS AGHQNAQTSI NWLFCGGDAA
MGAASVVEAI GEGEKAAVGI DEYLTGANHA FWREDVPVDT YFDPDEEPKN YPRKKMELLS
IERRINSFAE VEQPWDKSEA IRQAQRCLRC DYGKYKCPAA KMQAGVE
//
